EcoliWiki - User contributions [en]

Category:GO:0045203 ! integral component of cell outer membrane

2015-08-05T00:24:09Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0045203_!_integral_component_of_cell_outer_membrane}}

==References==
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Category:GO:0008891 ! glycolate oxidase activity

2015-08-05T00:10:43Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0008891_!_glycolate_oxidase_activity}}

==References==
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Category:GO:0015809 ! arginine transport

2015-08-04T23:26:04Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0015809_!_arginine_transport}}

==References==
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PMID:8554505

2015-08-04T23:12:51Z

68.180.230.156: Fill PMID: Page!

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{| id="Z55c146f2882fa" class=" tableEdit PMID_info_table"

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'''Cozier, GE and Anthony, C''' (1995) Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. ''Biochem. J.'' '''312 ( Pt 3)''':679-85
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!align=left |Abstract
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The structure of methanol dehydrogenase (MDH) at 0.194 nm (1.94 A) has been used to provide a model structure for part of a membrane quinoprotein glucose dehydrogenase (GDH). The basic superbarrel structure is retained, along with the tryptophan-docking motifs. The active-site regions are similar, but there are important differences, the most important being that GDH lacks the novel disulphide ring structure formed from adjacent cysteines in MDH; in GDH the equivalent region is occupied by His-262. Because of the overall similarities in the active-site region, the mechanism of action of GDH is likely to be similar to that of MDH. The differences in co-ordination to the cation and bonding to the pyrrolo-quinoline quinone (PQQ) in the active site may explain the relative ease of dissociation of the prosthetic group from the holo-GDH. There are considerable differences in the external loops, particularly those involved in formation of the shallow funnel leading to the active site, the configuration of which influences substrate specificity. The proposed model is consistent in many respects with previous proposals for the active-site structure based on the effects of chemical modification on binding of PQQ and enzymic activity.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8554505 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1136167 PMC1136167]

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!align=left |Keywords
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Alcohol Oxidoreductases/chemistry; Amino Acid Sequence; Binding Sites; Consensus Sequence; Escherichia coli/enzymology; Glucose Dehydrogenases/chemistry; Gram-Negative Aerobic Bacteria/enzymology; Models, Molecular; Molecular Sequence Data; PQQ Cofactor; Quinolones/metabolism

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PMID:8554505

2015-08-04T23:12:50Z

68.180.230.156: New PMID: Page!

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Category:GO:0048039 ! ubiquinone binding

2015-08-04T23:11:05Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0048039_!_ubiquinone_binding}}

==References==
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Category:GO:0008876 ! quinoprotein glucose dehydrogenase activity

2015-08-04T23:08:49Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0008876_!_quinoprotein_glucose_dehydrogenase_activity}}

==References==
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PMID:1312028

2015-08-04T22:38:02Z

68.180.230.156: Fill PMID: Page!

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{| id="O55c13ec98cefd" class=" tableEdit PMID_info_table"

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!align=left |Citation
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'''Werth, MT, Sices, H, Cecchini, G, Schröder, I, Lasage, S, Gunsalus, RP and Johnson, MK''' (1992) Evidence for non-cysteinyl coordination of the [2Fe-2S] cluster in Escherichia coli succinate dehydrogenase. ''FEBS Lett.'' '''299''':1-4
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!align=left |Abstract
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The consequences of replacing Cys65 in the FrdB subunit of Escherichia coli fumarate reductase by Asp or Ala have been investigated in terms of bacterial growth, enzymatic activity, and the ERP/redox properties of the [2Fe-2S] cluster. An aspartic acid residue occupies the equivalent position in E. coli succinate dehydrogenase, and the FrdBCys65Asp mutation has little effect on cell growth, enzyme activity or the physical properties of the Frd [2Fe-2S] cluster. In contrast, the [2Fe-2S] cluster was not observed in the FrdBCys65Ala mutant showing that a coordinating residue is required at this position for assembly of this cluster and significant levels of enzymatic activity. These results support the presence of one non-cysteinyl, oxygenic ligand for the [2Fe-2S] cluster in E. coli succinate dehydrogenase.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1312028 PubMed]

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!align=left |Keywords
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Cysteine/chemistry; Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology; Escherichia coli/growth & development; Iron/chemistry; Oxidation-Reduction; Succinate Dehydrogenase/chemistry; Succinate Dehydrogenase/metabolism; Sulfur/chemistry

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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PMID:1312028

2015-08-04T22:38:01Z

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PMID:2987185

2015-08-04T22:36:02Z

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{| id="E55c13e51a8dae" class=" tableEdit PMID_info_table"

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'''Magnusson, K, Hederstedt, L and Rutberg, L''' (1985) Cloning and expression in Escherichia coli of sdhA, the structural gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex. ''J. Bacteriol.'' '''162''':1180-5
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!align=left |Abstract
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Bacillus subtilis cytochrome b558 is a transmembrane protein which anchors succinate dehydrogenase (SDH) to the cytoplasmic membrane and is reduced by succinate. The structural gene for this cytochrome was cloned and expressed in Escherichia coli. Random BamHI or BglII fragments of B. subtilis 168 DNA were cloned in the BamHI site of plasmid pHV32. The derived plasmids were used to transform B. subtilis SDH mutants to chloramphenicol resistance by integration of the plasmid via DNA homology. Of some 3,000 transformants tested, 6 were SDH positive and had pHV32 integrated close to the sdh operon. Two plasmids, pKIM2 and pKIM4, with an insert of B. subtilis DNA of 5.7 and 3.4 kilobases, respectively, were generated by transforming E. coli with DNA from the SDH-positive transformants after cleavage with EcoRI or BglII and ligation. In E. coli carrying either of the two plasmids, about 4% of total membrane protein was B. subtilis cytochrome b558. E. coli (pKIM2) also contained antigen which reacted with antibodies specific for the flavoprotein and the iron-sulfur protein subunit of B. subtilis SDH. Enzymatically active, membrane-bound B. subtilis SDH could not be demonstrated in E. coli (pKIM2). The B. subtilis DNA insert in pKIM2 could transform B. subtilis sdhA (cytochrome b558), sdhB (flavoprotein), and sdhC (iron-sulfur protein) mutants to the wild type. The results suggest that pKIM2 carries the whole B. subtilis sdh operon. The data confirm the gene order and the proposed direction of transcription of the B. subtilis sdh operon. Most likely the sdh genes in E. coli(pKIM2) are controlled by their natural promoter.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2987185 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC215901 PMC215901]

|-
!align=left |Keywords
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Antigens, Bacterial/analysis; Bacillus subtilis/enzymology; Bacillus subtilis/genetics; Cloning, Molecular; Cytochrome b Group/genetics; DNA Transposable Elements; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; NADPH Oxidase; Operon; Succinate Dehydrogenase/genetics

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==Significance {{HelpIcon|Help:Literature}} ==
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==References==
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PMID:2987185

2015-08-04T22:36:01Z

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PMID:2997176

2015-08-04T22:35:43Z

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{| id="C55c13e3f54746" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
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'''Morningstar, JE, Johnson, MK, Cecchini, G, Ackrell, BA and Kearney, EB''' (1985) The high potential iron-sulfur center in Escherichia coli fumarate reductase is a three-iron cluster. ''J. Biol. Chem.'' '''260''':13631-8
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!align=left |Abstract
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The fumarate reductase complex and soluble enzyme from Escherichia coli have been investigated by low temperature magnetic circular dichroism and electron paramagnetic resonance spectroscopies. The results confirm the presence of one [2Fe-2S] cluster and show that the high potential iron-sulfur center is a 3Fe cluster of the type found in bacterial ferredoxins. Since the 3Fe cluster is present in catalytically competent enzyme and does not appear to be involved in any type of cluster conversion under reducing conditions, we conclude that it is an intrinsic component of the functional enzyme. The significance of the results is discussed in relation to the published amino acid sequence and the iron-sulfur cluster composition of bacterial fumarate reductases.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2997176 PubMed]

|-
!align=left |Keywords
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Amino Acid Sequence; Circular Dichroism; Cysteine/analysis; Dithionite/pharmacology; Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology; Iron-Sulfur Proteins/analysis; Metalloproteins/analysis; Multienzyme Complexes/analysis; Succinate Dehydrogenase/analysis; Temperature

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==Significance {{HelpIcon|Help:Literature}} ==
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PMID:2997176

2015-08-04T22:35:43Z

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PMID:16864590

2015-08-04T22:35:29Z

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{| id="M55c13e30e2a14" class=" tableEdit PMID_info_table"

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'''Cheng, VW, Ma, E, Zhao, Z, Rothery, RA and Weiner, JH''' (2006) The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow. ''J. Biol. Chem.'' '''281''':27662-8
|-
!align=left |Abstract
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Succinate dehydrogenase is an indispensable enzyme involved in the Krebs cycle as well as energy coupling in the mitochondria and certain prokaryotes. During catalysis, succinate oxidation is coupled to ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer. Hydrophobic residues around the [4Fe-4S] cluster were mutated to determine their effects on the midpoint potential of the cluster as well as electron transfer rates. SdhB-I150E and SdhB-I150H mutants lowered the midpoint potential of this cluster; surprisingly, the His variant had a lower midpoint potential than the Glu mutant. Mutation of SdhB-Leu-220 to Ser did not alter the redox behavior of the cluster but instead lowered the midpoint potential of the [3Fe-4S] cluster. To correlate the midpoint potential changes in these mutants to enzyme function, we monitored aerobic growth in succinate minimal medium, anaerobic growth in glycerol-fumarate minimal medium, non-physiological and physiological enzyme activities, and heme reduction. It was discovered that a decrease in midpoint potential of either the [4Fe-4S] cluster or the [3Fe-4S] cluster is accompanied by a decrease in the rate of enzyme turnover. We hypothesize that this occurs because the midpoint potentials of the [Fe-S] clusters in the native enzyme are poised such that direction of electron transfer from succinate to ubiquinone is favored.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16864590 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M604900200 10.1074/jbc.M604900200]
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!align=left |Keywords
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Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli/enzymology; Fumarates/chemistry; Iron-Sulfur Proteins/chemistry; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Plasmids/metabolism; Protein Structure, Quaternary; Reactive Oxygen Species; Succinate Dehydrogenase/chemistry; Ubiquinone/chemistry

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==References==
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PMID:16864590

2015-08-04T22:35:28Z

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PMID:20543070

2015-08-04T21:46:58Z

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{| id="B55c132d1a91f0" class=" tableEdit PMID_info_table"

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'''Lee, C, Kim, I, Lee, J, Lee, KL, Min, B and Park, C''' (2010) Transcriptional activation of the aldehyde reductase YqhD by YqhC and its implication in glyoxal metabolism of Escherichia coli K-12. ''J. Bacteriol.'' '''192''':4205-14
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!align=left |Abstract
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The reactive alpha-oxoaldehydes such as glyoxal (GO) and methylglyoxal (MG) are generated in vivo from sugars through oxidative stress. GO and MG are believed to be removed from cells by glutathione-dependent glyoxalases and other aldehyde reductases. We isolated a number of GO-resistant (GO(r)) mutants from Escherichia coli strain MG1655 on LB plates containing 10 mM GO. By tagging the mutations with the transposon TnphoA-132 and determining their cotransductional linkages, we were able to identify a locus to which most of the GO(r) mutations were mapped. DNA sequencing of the locus revealed that it contains the yqhC gene, which is predicted to encode an AraC-type transcriptional regulator of unknown function. The GO(r) mutations we identified result in missense changes in yqhC and were concentrated in the predicted regulatory domain of the protein, thereby constitutively activating the product of the adjacent gene yqhD. The transcriptional activation of yqhD by wild-type YqhC and its mutant forms was established by an assay with a beta-galactosidase reporter fusion, as well as with real-time quantitative reverse transcription-PCR. We demonstrated that YqhC binds to the promoter region of yqhD and that this binding is abolished by a mutation in the potential target site, which is similar to the consensus sequence of its homolog SoxS. YqhD facilitates the removal of GO through its NADPH-dependent enzymatic reduction activity by converting it to ethadiol via glycolaldehyde, as detected by nuclear magnetic resonance, as well as by spectroscopic measurements. Therefore, we propose that YqhC is a transcriptional activator of YqhD, which acts as an aldehyde reductase with specificity for certain aldehydes, including GO.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20543070 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2916428 PMC2916428]
Online version:[http://dx.doi.org/10.1128/JB.01127-09 10.1128/JB.01127-09]
|-
!align=left |Keywords
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Acetaldehyde/analogs & derivatives; Acetaldehyde/metabolism; Aldehyde Reductase/biosynthesis; Amino Acid Sequence; Artificial Gene Fusion; Binding Sites/genetics; DNA Mutational Analysis; DNA Transposable Elements; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; Drug Resistance, Bacterial; Escherichia coli K12/drug effects; Escherichia coli K12/metabolism; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; Genes, Reporter; Genetic Linkage; Glyoxal/metabolism; Glyoxal/toxicity; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation, Missense; NADP/metabolism; Protein Binding; Reverse Transcriptase Polymerase Chain Reaction; Sequence Analysis, DNA; Trans-Activators/metabolism; Transcription Factors/metabolism; Transcriptional Activation; Transduction, Genetic; beta-Galactosidase/genetics; beta-Galactosidase/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
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<annotationlinks/>

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==References==
{{RefHelp}}
<references/>

PMID:20543070

2015-08-04T21:46:57Z

68.180.230.156: New PMID: Page!

PMID on Demand placeholder

Category:GO:0015666 ! restriction endodeoxyribonuclease activity

2015-08-04T20:58:45Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0015666_!_restriction_endodeoxyribonuclease_activity}}

==References==
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Category:GO:0071978 ! bacterial-type flagellar swarming motility

2015-08-04T20:25:44Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0071978_!_bacterial-type_flagellar_swarming_motility}}

==References==
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Category:GO:0009750 ! response to fructose

2015-08-04T20:04:50Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0009750_!_response_to_fructose}}

==References==
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Category:GO:0047631 ! ADP-ribose diphosphatase activity

2015-08-04T19:39:56Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0047631_!_ADP-ribose_diphosphatase_activity}}

==References==
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Category:GO:0006268 ! DNA unwinding

2015-08-04T19:17:09Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0006268_!_DNA_unwinding}}

==References==
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Category:GO:0031365 ! N-terminal protein amino acid modification

2015-08-04T18:51:20Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0031365_!_N-terminal_protein_amino_acid_modification}}

==References==
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Category:GO:0008733 ! L-arabinose isomerase activity

2015-08-04T17:28:01Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0008733_!_L-arabinose_isomerase_activity}}

==References==
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PMID:2991272

2015-08-04T16:37:04Z

68.180.230.156: Fill PMID: Page!

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{| id="O55c0ea2fef27d" class=" tableEdit PMID_info_table"

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!align=left |Citation
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'''Freedman, R, Gibson, B, Donovan, D, Biemann, K, Eisenbeis, S, Parker, J and Schimmel, P''' (1985) Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts. ''J. Biol. Chem.'' '''260''':10063-8
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!align=left |Abstract
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Histidine-tRNA synthetase is one of the smallest bacterial aminoacyl-tRNA synthetases. It is less than one-half the size of the largest aminoacyl-tRNA synthetases. The entire nucleotide sequence of the Escherichia coli hisS locus was determined. The coding region is comprised of 424 codons, and the sequence was determined for 200 nucleotides on the 5'- and 3'-sides of the coding region. The translated nucleotide sequence was confirmed extensively by independent amino acid sequence information obtained by Edman degradations of purified peptides and by measurements of peptide masses by fast atom bombardment mass spectrometry. A significant sequence alignment of four bacterial aminoacyl-tRNA synthetases was reported recently (Webster, T., Tsai, H., Kula, M., Mackie, G., and Schimmel, P. (1984) Science 226, 1315-1317). Although the four enzymes vary considerably in length, this match occurs within the first 100 amino acids of each of the four enzymes and is in the segment believed to be part of the catalytic core. But no strong alignment could be found of the histidine sequence with these four tRNA synthetase sequences. This enzyme may be derived, therefore, from a different progenitor. Previous work suggested that three places in the hisS 5'-noncoding sequence could be promoter sites for RNA polymerase (Eisenbeis, S. J., and Parker, J. (1982) Gene 18, 107-114). We detected a 1400-nucleotide RNA species by RNA blot analysis with a hisS-specific probe. S1 nuclease mapping demonstrated a 5'-end to the RNA species occurs at -67 +/- 1, relative to the first nucleotide of the coding region. This position coincides with the predicted start site for transcription from one of the previously proposed promoter sites.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2991272 PubMed]

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!align=left |Keywords
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Amino Acid Sequence; Amino Acyl-tRNA Synthetases/genetics; Base Sequence; Codon; DNA Restriction Enzymes; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Histidine-tRNA Ligase/genetics; Protein Biosynthesis; Transcription, Genetic

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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<annotationlinks/>

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==References==
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PMID:2991272

2015-08-04T16:37:03Z

68.180.230.156: New PMID: Page!

PMID on Demand placeholder

Category:GO:0003955 ! NAD(P)H dehydrogenase (quinone) activity

2015-08-04T16:33:47Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0003955_!_NAD(P)H_dehydrogenase_(quinone)_activity}}

==References==
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Category:GO:0009379 ! Holliday junction helicase complex

2015-08-04T14:29:31Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0009379_!_Holliday_junction_helicase_complex}}

==References==
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Category:GO:0050440 ! 2-methylcitrate synthase activity

2015-08-04T13:52:07Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0050440_!_2-methylcitrate_synthase_activity}}

==References==
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Category:GO:0015893 ! drug transport

2015-08-04T13:04:14Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0015893_!_drug_transport}}

==References==
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Category:GO:0043590 ! bacterial nucleoid

2015-08-04T12:15:37Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0043590_!_bacterial_nucleoid}}

==References==
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Category:GO:0022417 ! protein maturation by protein folding

2015-08-04T11:42:11Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0022417_!_protein_maturation_by_protein_folding}}

==References==
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Category:GO:0070814 ! hydrogen sulfide biosynthetic process

2015-08-04T11:22:30Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0070814_!_hydrogen_sulfide_biosynthetic_process}}

==References==
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PMID:58966

2015-08-04T11:16:52Z

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'''Bailey, L, Ball, BV and Woods, RD''' (1976) An iridovirus from bees. ''J. Gen. Virol.'' '''31''':459-61
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!align=left |Abstract
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An iridovirus, Apis iridescent virus (AIV), isolated from sick adult specimens of Apis cerana (Hymenoptera) from Kashmir, closely resembles iridescent viruses from Tipula and Sericesthis spp. (TIV and SIV). However, AIV is only distantly related serologically to TIV and SIV and is even more remotely related to several other similar viruses that were tested in tube precipitation tests with intact particles. AIV multiplies in Apis mellifera, forming cytoplasmic iridescent crystalline aggregates in several tissues, but unlike all the other iridoviruses tested, it failed to multiply in Galleria mellonella.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=58966 PubMed]

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!align=left |Keywords
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Animals; Antigens, Viral/analysis; Bees/microbiology; Crystallography; Cytoplasm/microbiology; DNA Viruses; DNA, Viral; Epitopes; Inclusion Bodies, Viral; Insect Viruses/growth & development; Insect Viruses/immunology; Insect Viruses/ultrastructure

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
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<references/>

PMID:58966

2015-08-04T11:16:51Z

68.180.230.156: New PMID: Page!

PMID on Demand placeholder

Category:GO:0015386 ! potassium:hydrogen antiporter activity

2015-08-04T11:06:46Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0015386_!_potassium:hydrogen_antiporter_activity}}

==References==
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Category:GO:0050418 ! hydroxylamine reductase activity

2015-08-04T11:02:47Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0050418_!_hydroxylamine_reductase_activity}}

==References==
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Category:GO:0008768 ! UDP-sugar diphosphatase activity

2015-08-04T09:47:08Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0008768_!_UDP-sugar_diphosphatase_activity}}

==References==
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Category:GO:0043493 ! viral terminase complex

2015-08-04T09:07:58Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0043493_!_viral_terminase_complex}}

==References==
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PMID:8751891

2015-08-04T07:27:28Z

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{| id="T55c069601ef21" class=" tableEdit PMID_info_table"

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'''Sweeney, NJ, Laux, DC and Cohen, PS''' (1996) Escherichia coli F-18 and E. coli K-12 eda mutants do not colonize the streptomycin-treated mouse large intestine. ''Infect. Immun.'' '''64''':3504-11
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!align=left |Abstract
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The Escherichia coli human fecal isolates F-18 and K-12 are excellent colonizers of the streptomycin-treated mouse intestine. E. coli F-18 and E. coli K-12 eda mutants (unable to utilize glucuronate, galacturonate, and gluconate) were constructed by insertional mutagenesis. Neither the E. coli F-18 eda nor the E. coli K-12 eda mutant was able to colonize the streptomycin-treated mouse intestine, whether they were fed to mice together with their respective parental strains or alone. Complementation of the eda mutants with pTC190 (containing a functional E. coli K-12 eda gene) completely restored the colonization ability of both eda mutants. Relative to their parental strains, the E. coli F-18 eda mutant and the E. coli K-12 eda mutant grew poorly in cecal mucus isolated from mice fed either normal mouse chow or a synthetic diet containing sucrose as the sole carbon source, yet the mutants and parental strains demonstrated identical growth rates in minimal medium with glucose as the carbon source. E. coli F-18 edd eda and E. coli K-12 edd eda double mutants colonized the streptomycin-treated intestine when fed to mice alone; however, when fed simultaneously with their respective parental strains, they were poor colonizers. Since the edd gene is involved only in gluconate metabolism via the Entner-Doudoroff pathway, these results implicate the utilization of gluconate and the Entner-Doudoroff pathway as important elements in E. coli colonization of the streptomycin-treated mouse large intestine.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8751891 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC174255 PMC174255]

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!align=left |Keywords
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Animals; Cecum/microbiology; Escherichia coli/genetics; Escherichia coli/pathogenicity; Genetic Complementation Test; Gluconates/metabolism; Glucuronates/metabolism; Glucuronic Acid; Hexuronic Acids/metabolism; Intestinal Mucosa/microbiology; Mice; Mice, Inbred Strains

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:8751891

2015-08-04T07:27:28Z

68.180.230.156: New PMID: Page!

PMID on Demand placeholder

Category:GO:0019294 ! keto-3-deoxy-D-manno-octulosonic acid biosynthetic process

2015-08-04T06:55:54Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0019294_!_keto-3-deoxy-D-manno-octulosonic_acid_biosynthetic_process}}

==References==
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Category:GO:0019299 ! rhamnose metabolic process

2015-08-04T06:55:42Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0019299_!_rhamnose_metabolic_process}}

==References==
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Category:GO:0009403 ! toxin biosynthetic process

2015-08-04T06:39:48Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0009403_!_toxin_biosynthetic_process}}

==References==
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Category:GO:0031405 ! lipoic acid binding

2015-08-04T02:58:53Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0031405_!_lipoic_acid_binding}}

==References==
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Category:GO:0019008 ! molybdopterin synthase complex

2015-08-04T01:50:10Z

68.180.230.156: New GO term category page

{{GO term stub|GO:0019008_!_molybdopterin_synthase_complex}}

==References==
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PMID:18337747

2015-08-04T00:48:14Z

68.180.230.156: Fill PMID: Page!

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{| id="G55c00bcdd68f1" class=" tableEdit PMID_info_table"

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'''Cohen-Ben-Lulu, GN, Francis, NR, Shimoni, E, Noy, D, Davidov, Y, Prasad, K, Sagi, Y, Cecchini, G, Johnstone, RM and Eisenbach, M''' (2008) The bacterial flagellar switch complex is getting more complex. ''EMBO J.'' '''27''':1134-44
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!align=left |Abstract
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The mechanism of function of the bacterial flagellar switch, which determines the direction of flagellar rotation and is essential for chemotaxis, has remained an enigma for many years. Here we show that the switch complex associates with the membrane-bound respiratory protein fumarate reductase (FRD). We provide evidence that FRD binds to preparations of isolated switch complexes, forms a 1:1 complex with the switch protein FliG, and that this interaction is required for both flagellar assembly and switching the direction of flagellar rotation. We further show that fumarate, known to be a clockwise/switch factor, affects the direction of flagellar rotation through FRD. These results not only uncover a new component important for switching and flagellar assembly, but they also reveal that FRD, an enzyme known to be primarily expressed and functional under anaerobic conditions in Escherichia coli, nonetheless, has important, unexpected functions under aerobic conditions.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18337747 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323253 PMC2323253]
Online version:[http://dx.doi.org/10.1038/emboj.2008.48 10.1038/emboj.2008.48]
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!align=left |Keywords
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Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli/ultrastructure; Flagella/enzymology; Flagella/metabolism; Flagella/ultrastructure; Fumarates/metabolism; Gene Deletion; Genes, Switch; Protein Binding; Recombinant Fusion Proteins/metabolism; Succinate Dehydrogenase/isolation & purification; Succinate Dehydrogenase/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:18337747

2015-08-04T00:48:13Z

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PMID on Demand placeholder

PMID:6985892

2015-08-04T00:32:54Z

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{| id="X55c0083687bfc" class=" tableEdit PMID_info_table"

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!align=left |Citation
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'''Higgins, W, Miles, EW and Fairwell, T''' (1980) Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli. ''J. Biol. Chem.'' '''255''':512-7
|-
!align=left |Abstract
||
The three known active site residues of the tryptophan synthase beta 2 subunit from Escherichia coli are shown to fall within 25 residues of each other in the primary sequence of the NH2-terminal region of the beta 2 subunit. These residues are: lysine-86, which forms a Schiff's base with pyridoxal phosphate; histidine-81 or histidine-85, which removes the alpha proton of L-serine; and cysteine-61, which reacts with bromoacetylpyridoxamine phosphate, an affinity label for the beta 2 subunit. The sequence of the first 78 residues of a single cyanogen bromide fragment containing these active site residues has been determined by automatic Edman degradation and by sequence analysis of daughter peptides. This 79-residue cyanogen bromide fragment, which contains the 22-residue pyridoxyl peptide sequenced earlier by Fluri et al. (Fluri, R., Jackson, L. E., Lee, W. E., and Crawford, I. P. (1971) J. Biol. Chem. 246, 6620-6624), was placed at the NH2-terminal end of the beta chain beginning at residue 22. Thus, the primary sequence of residues 1 to 99 of the beta 2 subunit is reported.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6985892 PubMed]

|-
!align=left |Keywords
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Amino Acid Sequence; Binding Sites; Cyanogen Bromide; Escherichia coli/enzymology; Macromolecular Substances; Peptide Fragments/analysis; Trypsin; Tryptophan Synthase/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:6985892

2015-08-04T00:32:54Z

68.180.230.156: New PMID: Page!

PMID on Demand placeholder