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PMID: 8431 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Ornithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase.

Journal of bacteriology ·Vol. 127 ·No. 3 ·1976-09-00 ·Pages 1315-23

Billheimer JT, Carnevale HN, Leisinger T, Eckhardt T, Jones EE

Abstract

Procedures that have been developed for the purification of acetylornithine delta-transaminase from Escherichia coli W also lead to the simultaneous purification of ornithine delta-transaminase. These two enzymatic activities have the same electrophoretic mobility and are identical immunochemically. Studies of inhibition kinetics demonstrate that the two substrates, acetylornithine and ornithine, compete for the same active site of acetylornithine delta-transaminase; thus, the ornithine delta-transaminase activity in E coli is due to acetylornithine delta-transaminase and not to a separate specific ornithine delta-transaminase.

MeSH Terms
Binding Sites Electrophoresis, Disc Enzyme Induction Enzyme Repression Escherichia coli/enzymology Hydrogen-Ion Concentration Immunoassay Kinetics Ornithine-Oxo-Acid Transaminase/biosynthesis,isolation & purification,metabolism Transaminases/biosynthesis,isolation & purification,metabolism
Chemicals
Transaminases Ornithine-Oxo-Acid Transaminase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Billheimer J T
Carnevale H N
Leisinger T
Eckhardt T
Jones E E
References (15)
15 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.127.3.1315-1323.1976
Published
1976-09-00
Pages
1315-23
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC232926
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.127.3.1315-1323.1976 PMC Full Text View journal details
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