PURIFICATION AND CHARACTERIZATION OF METHYLGLYOXAL REDUCTASE FROM HANSENULA-MRAKII

被引:7
作者
INOUE, Y [1 ]
TRAN, LT [1 ]
YOSHIKAWA, K [1 ]
MURATA, K [1 ]
KIMURA, A [1 ]
机构
[1] KYOTO UNIV, FOOD SCI RES INST, UJI, KYOTO 611, JAPAN
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1991年 / 71卷 / 02期
关键词
D O I
10.1016/0922-338X(91)90240-H
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Methylglyoxal reductase was purified from Hansenula mrakii IFO 0895 to a homogenous state on polyacrylamide gel electrophoresis. The enzyme consisted of a single polypeptide chain with a molecular weight of 34,000. The enzyme was specific to methylglyoxal (K(m) = 1.92 mM) and NADPH (K(m) = 40.8-mu-M). The activity of the enzyme was inhibited by p-chloromercuribenzoate and HgCl2. NADP also inhibited the activity of the enzyme, and the K(i) value was calculated to be 0.25 mM.
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收藏
页码:134 / 136
页数:3
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