Literature DB >> 2516870

Evolutionary relationships among bacterial carbamoyltransferases.

C Tricot1, J L De Coen, P Momin, P Falmagne, V Stalon.   

Abstract

An immunological approach was used for the study of ornithine carbamoyltransferase (OTCase) evolution in bacteria. Antisera were prepared against the anabolic and catabolic OTCases of Pseudomonas aeruginosa and Aeromonas formicans as well as against OTCase and putrescine carbamoyltransferases from Streptococcus faecalis; these antisera were then tested against the unpurified OTCases, either anabolic or catabolic, of 34 bacterial strains. Extensive cross-reactions were observed between the antisera to catabolic OTCases from P. aeruginosa, A. formicans and S. faecalis and the catabolic enzymes from other species or genera. These antisera cross-reacted also with the anabolic OTCases of strains of the Enterobacteriaceae but not with the anabolic OTCases of the same species or of other species or genera. The cross-reaction measured between the antisera against P. aeruginosa anabolic OTCase and the anabolic OTCases of other Pseudomonas were largely in agreement with the phylogenic subdivision of Pseudomonas proposed by N. J. Palleroni. The correlation was also significantly higher with the anabolic enzyme of an archaeobacterium, Methanobacterium thermoaceticum, than with the catabolic or anabolic OTCases from other genera in the eubacterial line. The antiserum raised against A. formicans anabolic OTCase was quite specific for its antigen and appeared to be raised against the heaviest of the various oligomeric structures of the enzyme.

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Year:  1989        PMID: 2516870     DOI: 10.1099/00221287-135-9-2453

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN: 0022-1287


  7 in total

1.  Origin, structure, and regulation of argK, encoding the phaseolotoxin-resistant ornithine carbamoyltransferase in Pseudomonas syringae pv. phaseolicola, and functional expression of argK in transgenic tobacco.

Authors:  E Hatziloukas; N J Panopoulos
Journal:  J Bacteriol       Date:  1992-09       Impact factor: 3.490

2.  Human ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changes.

Authors:  D Shi; H Morizono; X Yu; L Tong; N M Allewell; M Tuchman
Journal:  Biochem J       Date:  2001-03-15       Impact factor: 3.857

3.  The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction.

Authors:  José L Llácer; Luis Mariano Polo; Sandra Tavárez; Benito Alarcón; Rebeca Hilario; Vicente Rubio
Journal:  J Bacteriol       Date:  2006-10-06       Impact factor: 3.490

4.  Crystal structure and biochemical properties of putrescine carbamoyltransferase from Enterococcus faecalis: Assembly, active site, and allosteric regulation.

Authors:  Dashuang Shi; Xiaolin Yu; Gengxiang Zhao; Jeremy Ho; Shennon Lu; Norma M Allewell; Mendel Tuchman
Journal:  Proteins       Date:  2012-02-13

5.  Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis.

Authors:  Hiroki Morizono; Juan Cabrera-Luque; Dashuang Shi; Rene Gallegos; Saori Yamaguchi; Xiaolin Yu; Norma M Allewell; Michael H Malamy; Mendel Tuchman
Journal:  J Bacteriol       Date:  2006-04       Impact factor: 3.490

6.  Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): purification, characterization, sequence determination, and evolution.

Authors:  A Ruepp; H N Müller; F Lottspeich; J Soppa
Journal:  J Bacteriol       Date:  1995-03       Impact factor: 3.490

7.  Retrieving sequences of enzymes experimentally characterized but erroneously annotated : the case of the putrescine carbamoyltransferase.

Authors:  Daniil G Naumoff; Ying Xu; Nicolas Glansdorff; Bernard Labedan
Journal:  BMC Genomics       Date:  2004-08-02       Impact factor: 3.969

  7 in total

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