| Literature DB >> 10570813 |
K Krüger1, G Lang, T Weidner, A M Engel.
Abstract
Nucleotide sequence and biochemical analysis of D-beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30), isolated from Rhodobacter sp., indicate functional oligomers composed of subunits of 257 amino acids with a calculated M(r) of 26,800 and a pI of 5.90. Compared to mammalian short-chain alcohol dehydrogenases, the bacterial enzyme lacks a C-terminal lipid anchor domain and was found to be highly active upon expression in Escherichia coli even without lipid supplement. The recombinant enzyme could be highly enriched using a single chromatography step and was shown to be stable over a broad range of pH and temperature.Entities:
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Year: 1999 PMID： 10570813 DOI： 10.1007/s002530051576
Source DB: PubMed Journal: Appl Microbiol Biotechnol ISSN： 0175-7598 Impact factor: 4.813