Allohydroxy-d-proline dehydrogenase
β Scribed by A. J. Bater; W. A. Venables; Susan Thomas
- Publisher
- Springer
- Year
- 1977
- Tongue
- English
- Weight
- 211 KB
- Volume
- 112
- Category
- Article
- ISSN
- 0302-8933
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β¦ Synopsis
G r o w t h of Pseudomonas aeruginosa PA01
on isomers of hydroxyproline induced the synthesis of an allohydroxy-D-proline dehydrogenase. The enzyme resembled the D-alanine dehydrogenase o f this organism in its association with the particulate fraction and its linkage to oxygen through a cytochromecontaining respiratory chain, but differed from this and other bacterial D-amino acid dehydrogenases in its high substrate specificity and low K,,.
π SIMILAR VOLUMES
The enzyme system from Clostridium sticklandii catalyzing the NADH-dependent reduction of D-proline was co-purified by chromatography on DEAE-cellulose at pH 8.2 and ammonium sulfate fractionation, and resolved into fractions containing three different protein components, NADH dehydrogenase, D-proli