| Literature DB >> 11717302 |
T Schräder1, G Zarnt, J R Andreesen.
Abstract
Different aldehyde dehydrogenases (AlDHs) were formed during growth of Ralstonia eutropha Bo on tetrahydrofurfuryl alcohol (THFA). One of these enzymes, AlDH 4, was purified and characterized as a homodimer containing no prosthetic groups, showing a strong substrate inhibition, and having an N-terminal sequence similar to those of various NAD(P)-dependent AlDHs. The conversion rate of THFA by the quinohemoprotein THFA dehydrogenase was increased by AlDH 4.Entities:
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Year: 2001 PMID: 11717302 PMCID: PMC95592 DOI: 10.1128/JB.183.24.7408-7411.2001
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490