PMID:15587: Difference between revisions

From EcoliWiki
Jump to navigation Jump to search
New PMID: Page!
 
imported>Wikientrybot
change PMID template to TableEdit version
 
(7 intermediate revisions by 2 users not shown)
Line 1: Line 1:
<protect>
{{RightTOC}}
{{RightTOC}}
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.130962.E52238a180faec-->
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="E52238a180faec"  class=" tableEdit PMID_info_table" 


<span style = 'font-size: large'> '''Applebaum, DM, Dunlap, JC and Morris, DR'''  (1977) Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli.''Biochemistry'' '''16''':1580-4</span>
|-
!align=left  |Citation
||
'''Applebaum, DM, Dunlap, JC and Morris, DR'''  (1977) Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli. ''Biochemistry'' '''16''':1580-4
|-
!align=left  |Abstract
||
Biosynthetic ornithine decarboxylase was purified 4300-fold from Escherichia coli to a purity of approximately 85% as judged by polyacrylamide gel electrophoresis. The enzyme showed hyperbolic kinetics with a Km of 5.6 mM for ornithine and 1.0 micronM for pyridoxal phosphate and it was competitively inhibited by putrescine and spermidine. The biosynthetic decarboxylase was compared with the biodegradative ornithine decarboxylase [Applebaum, D., et al. (1975), Biochemistry 14, 3675]. Both enzymes were dimers of 80 000-82 000 molecular weight and exhibited similar kinetic properties. However, they differed significantly in other respects. The pH optimum of the biosynthetic enzyme was 8.1, compared with 6.9 for the biodegradative. Both enzymes were activated by nucleotides, but with different specificity. Antibody to the purified biodegradative ornithine decarboxylase did not cross-react with the biosynthetic enzyme. The evolutionary relationship of these two decarboxylases to the other amino acid decarboxylases of E. coli is discussed.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15587 PubMed]


{|{{Prettytable}} align = 'center' width= '70%'
|-
|-
|{{TableHeadingColor}} |'''Abstract''' || Biosynthetic ornithine decarboxylase was purified 4300-fold from Escherichia coli to a purity of approximately 85% as judged by polyacrylamide gel electrophoresis. The enzyme showed hyperbolic kinetics with a Km of 5.6 mM for ornithine and 1.0 micronM for pyridoxal phosphate and it was competitively inhibited by putrescine and spermidine. The biosynthetic decarboxylase was compared with the biodegradative ornithine decarboxylase [Applebaum, D., et al. (1975), Biochemistry 14, 3675]. Both enzymes were dimers of 80 000-82 000 molecular weight and exhibited similar kinetic properties. However, they differed significantly in other respects. The pH optimum of the biosynthetic enzyme was 8.1, compared with 6.9 for the biodegradative. Both enzymes were activated by nucleotides, but with different specificity. Antibody to the purified biodegradative ornithine decarboxylase did not cross-react with the biosynthetic enzyme. The evolutionary relationship of these two decarboxylases to the other amino acid decarboxylases of E. coli is discussed.
!align=left  |Keywords
</noinclude>
||
|-
Carboxy-Lyases/metabolism; Chromatography; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Hydroxyapatites; Immunodiffusion; Isoenzymes/isolation & purification; Isoenzymes/metabolism; Kinetics; Molecular Weight; Ornithine Decarboxylase/isolation & purification; Ornithine Decarboxylase/metabolism; Putrescine/pharmacology; Ribonucleotides/pharmacology; Spermidine/pharmacology
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15587 PubMed]
 
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.130962.E52238a180faec&page=130962&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
|}
</protect>
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.130962.E52238a180faec-->
==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}
Line 19: Line 38:


==Annotations {{HelpIcon|Help:Literature}}==
==Annotations {{HelpIcon|Help:Literature}}==
<protect><!--box uid=63ce1649aab8b3180235b0af7618f667.0.H47ab59106ddab-->
<annotationlinks/>
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|class = 'sortable' {{Prettytable}} id='238786'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.H47ab59106ddab&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
<!--box uid=63ce1649aab8b3180235b0af7618f667.0.H47ab59106ddab--></protect>


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

Latest revision as of 04:26, 15 September 2013

Citation

Applebaum, DM, Dunlap, JC and Morris, DR (1977) Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli. Biochemistry 16:1580-4

Abstract

Biosynthetic ornithine decarboxylase was purified 4300-fold from Escherichia coli to a purity of approximately 85% as judged by polyacrylamide gel electrophoresis. The enzyme showed hyperbolic kinetics with a Km of 5.6 mM for ornithine and 1.0 micronM for pyridoxal phosphate and it was competitively inhibited by putrescine and spermidine. The biosynthetic decarboxylase was compared with the biodegradative ornithine decarboxylase [Applebaum, D., et al. (1975), Biochemistry 14, 3675]. Both enzymes were dimers of 80 000-82 000 molecular weight and exhibited similar kinetic properties. However, they differed significantly in other respects. The pH optimum of the biosynthetic enzyme was 8.1, compared with 6.9 for the biodegradative. Both enzymes were activated by nucleotides, but with different specificity. Antibody to the purified biodegradative ornithine decarboxylase did not cross-react with the biosynthetic enzyme. The evolutionary relationship of these two decarboxylases to the other amino acid decarboxylases of E. coli is discussed.

Links

PubMed

Keywords

Carboxy-Lyases/metabolism; Chromatography; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Hydroxyapatites; Immunodiffusion; Isoenzymes/isolation & purification; Isoenzymes/metabolism; Kinetics; Molecular Weight; Ornithine Decarboxylase/isolation & purification; Ornithine Decarboxylase/metabolism; Putrescine/pharmacology; Ribonucleotides/pharmacology; Spermidine/pharmacology

edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

<annotationlinks/>

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.

Retrieved from "https://ecoliwiki.org/colipedia/index.php?title=PMID:15587&oldid=1459510"