In:
Bioscience, Biotechnology, and Biochemistry, Informa UK Limited, Vol. 80, No. 8 ( 2016-08-02), p. 1536-1545
Kurzfassung:
The report is the first of purification, overproduction, and characterization of a unique γ-butyrobetainyl CoA synthetase from soil-isolated Agrobacterium sp. 525a. The primary structure of the enzyme shares 70–95% identity with those of ATP-dependent microbial acyl-CoA synthetases of the Rhizobiaceae family. As distinctive characteristics of the enzyme of this study, ADP was released in the catalytic reaction process, whereas many acyl CoA synthetases are annotated as an AMP-forming enzyme. The apparent Km values for γ-butyrobetaine, CoA, and ATP were, respectively, 0.69, 0.02, and 0.24 mM.
Materialart:
Online-Ressource
ISSN:
0916-8451
,
1347-6947
DOI:
10.1080/09168451.2016.1177447
Sprache:
Englisch
Verlag:
Informa UK Limited
Publikationsdatum:
2016
ZDB Id:
2110940-0
SSG:
12
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