| Literature DB >> 3135803 |
S A Murrell1, R G Lowery, P W Ludden.
Abstract
The effect of ADP-ribosylation of dinitrogenase reductase on its binding to dinitrogenase was investigated. Dinitrogenase reductase from Clostridium pasteurianum (Cp2) was a substrate for the ADP-ribosyltransferase and the dinitrogenase-reductase-activating glycohydrolase from Rhodospirillum rubrum. ADP-ribosylation inactivated Cp2 and prevented its formation of a tight complex with dinitrogenase from Azotobacter vinelandii (Av1). The complex between Cp2 and Av1 could not be ADP-ribosylated once it formed.Entities:
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Year: 1988 PMID: 3135803 PMCID: PMC1149044 DOI: 10.1042/bj2510609
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857