|
type |
Journal Article |
authors |
Wada H, Snell EE |
title |
Enzymatic transamination of pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase.
|
journal |
J Biol Chem |
Activity |
2.6.1.30 |
Family |
2.6.1.30 |
sel |
unselected |
ui |
14004227 |
year |
(1962) |
volume |
237 |
number |
1 |
pages |
133-7 |
| |
abstract |
Previous reports from this laboratory have described the isolation and characterization of several metabolites formed during the oxidative degradation of pyridoxine (2, 3) and of pyridoxamine (4) by certain soil pseudomonads. Although one of these organisms, Pseudomonas sp. MA, forms pyridoxal from pyridoxamine as the first step in degradation of the latter compound, we were unable to demonstrate oxidative deamination of pyridoxamine in cell-free extracts. About this time, the occurrence of pyridoxamine-oxaloacetic transaminase in cstracts of Escherichia coli and rabbit liver was discovered (1). Appropriate tests revealed a much more active pyridoxamine transaminase, apparently specific for pyruvate as amino group acceptor, in cells of Pseudomonas sp. MA grown on pyridoxamine as a source of carbon and nitrogen. The purification and certain properties of this enzyme are described herein.
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last changed |
2017/12/14 11:41 |
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