Details
| Original language | English |
|---|---|
| Pages (from-to) | 2006-2008 |
| Number of pages | 3 |
| Journal | Journal of the Chemical Society. Perkin Transactions 1 |
| Volume | 1 |
| Issue number | 17 |
| Publication status | Published - 1 Jan 2001 |
| Externally published | Yes |
Abstract
We examined the similarities and differences between the activities of N-succinyl-ll-diaminopimelate aminotransferase (DAP-AT) and N-acetylornithine aminotransferase (NAcO-AT) from E. coli and M. smegmatis in order to investigate recent claims that the two enzymes are one and the same. The results do not support the hypothesis that the two activities are catalysed by a single enzyme.
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
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In: Journal of the Chemical Society. Perkin Transactions 1, Vol. 1, No. 17, 01.01.2001, p. 2006-2008.
Research output: Contribution to journal › Comment/debate › Research › peer review
}
TY - JOUR
T1 - Is N-acetylornithine aminotransferase the real N-succinyl-ll-diaminopimelate aminotransferase in Escherichia coli and Mycobacterium smegmatis?
AU - Cox, Russell J.
AU - Wang, Paul S.H.
PY - 2001/1/1
Y1 - 2001/1/1
N2 - We examined the similarities and differences between the activities of N-succinyl-ll-diaminopimelate aminotransferase (DAP-AT) and N-acetylornithine aminotransferase (NAcO-AT) from E. coli and M. smegmatis in order to investigate recent claims that the two enzymes are one and the same. The results do not support the hypothesis that the two activities are catalysed by a single enzyme.
AB - We examined the similarities and differences between the activities of N-succinyl-ll-diaminopimelate aminotransferase (DAP-AT) and N-acetylornithine aminotransferase (NAcO-AT) from E. coli and M. smegmatis in order to investigate recent claims that the two enzymes are one and the same. The results do not support the hypothesis that the two activities are catalysed by a single enzyme.
UR - http://www.scopus.com/inward/record.url?scp=0034827204&partnerID=8YFLogxK
U2 - 10.1039/b106146c
DO - 10.1039/b106146c
M3 - Comment/debate
AN - SCOPUS:0034827204
VL - 1
SP - 2006
EP - 2008
JO - Journal of the Chemical Society. Perkin Transactions 1
JF - Journal of the Chemical Society. Perkin Transactions 1
SN - 1472-7781
IS - 17
ER -