EcoliWiki - User contributions [en]

PMID:4562390

2017-07-31T14:06:51Z

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'''Vonder Haar, RA and Umbarger, HE''' (1972) Isoleucine and valine metabolism in Escherichia coli. XIX. Inhibition of isoleucine biosynthesis by glycyl-leucine. ''J. Bacteriol.'' '''112''':142-7
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!align=left |Abstract
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The inhibition of growth of the K-12 strain of Escherichia coli by glycyl-l-leucine observed originally by Simmonds and co-workers was investigated. The inhibition was reversed by isoleucine and those precursors of isoleucine beyond threonine in the biosynthetic pathway. Threonine reversed the inhibition poorly. With heavy cell suspensions, the inhibition was transient: the onset of growth followed the disappearance of the dipeptide from the medium and the appearance of glycine and leucine. Glycyl-leucine was shown to be an inhibitor of threonine deaminase (EC 4.2.1.16 l-threonine hydro-lyase [deaminating]). One kind of glycyl-leucine-resistant mutant had a threonine deaminase that was resistant to isoleucine and glycyl-leucine inhibition. The pattern of glycyl-leucine inhibition is compared with those of inhibition by isoleucine and by the weaker inhibitors leucine and valine.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4562390 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC251389 PMC251389]

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Acylation; Cell-Free System; Chloramphenicol/pharmacology; Culture Media; Dipeptides/pharmacology; Drug Resistance, Microbial; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/growth & development; Escherichia coli/metabolism; Glycine/pharmacology; Hydro-Lyases/metabolism; Isoleucine/antagonists & inhibitors; Isoleucine/biosynthesis; Isoleucine/pharmacology; Leucine/pharmacology; Lyases/metabolism; Mutation; Operon; Pyruvates; Rifampin/pharmacology; Threonine; Valine/biosynthesis; Valine/pharmacology

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PMID:4562390

2017-07-31T14:06:50Z

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PMID:4872216

2017-07-31T13:27:29Z

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'''Weber, K''' (1968) New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain. ''Nature'' '''218''':1116-9
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No abstract in PubMed
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4872216 PubMed]

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Amino Acid Sequence; Escherichia coli/enzymology; Models, Structural; Molecular Weight; Transferases/analysis

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

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
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PMID:4872216

2017-07-31T13:27:28Z

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PMID:19494579

2016-09-02T20:19:59Z

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'''Lengeler, JW and Jahreis, K''' (2009) Bacterial PEP-dependent carbohydrate: phosphotransferase systems couple sensing and global control mechanisms. ''Contrib Microbiol'' '''16''':65-87
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The PEP-dependent carbohydrate:phosphotransferase systems (PTSs) of enteric bacteria constitute a complex sensory system which involves as its central element a PEP-dependent His-protein kinase (Enzyme I). As a unit, the PTS comprises up to 20 different transporters per cell which correspond to its chemoreceptors for PTS carbohydrates, and several targeting subunits, which include in the low [G+C] Gram-positive bacteria an ancillary Ser/Thr-protein kinase. The PTS senses the presence of carbohydrates, in particular glucose, in the medium and the energy state of the cell, in the form of either the intracellular PEP-to-pyruvate ratio or the D-fructose-bisphosphate levels. This information is subsequently communicated to cellular targets, in particular those involved in the chemotactic response of the cell towards PTS carbohydrates, and in sensing glucose in the medium, using cAMP and several targeting subunits as intermediates. Peptide targeting subunits ensure the fast, transient, and yet accurate communication of the PTS with its more than hundred different targets, avoiding at the same time unwanted cross-talk. Many elements of this sensory system are simultaneously elements of specific and global regulatory networks. Thus, the PTS controls, besides the immediate (in the ms to s range) chemotactic responses, the activity of the various carbohydrate transporters and enzymes involved in carbon and energy metabolism through inducer exclusion, and in a delayed response (in the min to h range) the synthesis of these transporters and catabolic enzymes through catabolite repression. Indirect consequences of this program are phenomena related to cell surface rearrangements, which include flagella synthesis, as well as memory, adaptation, and learning effects. The analogy between the PTS and other prokaryotic systems, and more complex sensory systems from eukaryotic organisms which share elements with regulatory systems is obvious.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19494579 PubMed]
Online version:[http://dx.doi.org/10.1159/000219373 10.1159/000219373]
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Bacterial Physiological Phenomena; Biological Transport; Carbohydrate Metabolism; Chemotaxis; Computer Simulation; Glucose/metabolism; Phosphoenolpyruvate/metabolism; Phosphoenolpyruvate Sugar Phosphotransferase System/physiology; Pyruvic Acid/metabolism; Quorum Sensing/physiology; Signal Transduction

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

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

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

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==See also==

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

PMID:19494579

2016-09-02T20:19:58Z

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Category:GO:0006729 ! tetrahydrobiopterin biosynthetic process

2015-09-16T01:58:20Z