Activities | Families | Sequences | Fold types | References | Help
B6db references: 2199330

type Journal Article
authors Heimberg, H.; Boyen, A.; Crabeel, M.; Glansdorff, N.
title Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase
journal Gene
sel selected
ui 2199330
year (1990)
volume 90
number 1
pages 69-78
keywords Amino Acid Sequence
abstract Genes argD and ARG8, encoding the acetylornithine aminotransferase (ACOAT) subunit in Escherichia coli and Saccharomyces cerevisiae, respectively, have been cloned and sequenced. The deduced amino acid sequences show substantial similarity. Moreover, they resemble ornithine aminotransferase (OAT) sequences (i.e., those from yeast, rat and man); the observed similarities are statistically significant, indicating that the enzymes are homologous. However, in contrast to OATs, which appear to be substrate (i.e., ornithine)-specific, S. cerevisiae ACOAT transaminates ornithine about as efficiently as E. coli does. The evolutionary relationship between ACOATs and OATs is discussed in terms of substrate ambiguity.
last changed 2009/04/15 13:22

B6db references