产气肠杆菌二乙酰（乙偶姻）还原酶的纯化、表征及一些性质

Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes.

作者信息

Carballo J, Martin R, Bernardo A, Gonzalez J

机构信息

Laboratory of Food Technology and Biochemistry, Facultad de Veterinaria, Universidad de León, Spain.

出版信息

Eur J Biochem. 1991 Jun 1;198(2):327-32. doi: 10.1111/j.1432-1033.1991.tb16019.x.

DOI:10.1111/j.1432-1033.1991.tb16019.x

PMID:2040298

Abstract

A new method, faster, milder and more efficient than the one previously described [Bryn, K., Hetland, O. & Stormer, F. C. (1971) Eur. J. Biochem, 18, 116-119], for purification of diacetyl(acetoin) reductase from Enterobacter aerogenes is proposed. The experiments carried out with the electrophoretically pure preparations obtained by this procedure show that the enzyme (a) produces L-glycols from the corresponding L-alpha-hydroxycarbonyls by reversible reduction of their oxo groups and also reduces the oxo group of uncharged alpha-dicarbonyls converting them into L-alpha-hydroxycarbonyls, and (b) is specific for NAD. This is a new enzyme for which we suggest the systematic name of L-glycol: NAD+ oxidoreductase and the recommended name of L-glycol dehydrogenase(NAD). The molecular mass, pI, affinity for substrates and pH profiles of this enzyme are also described.

摘要

本文提出了一种新的方法，用于从产气肠杆菌中纯化双乙酰（乙偶姻）还原酶，该方法比先前描述的方法[Bryn, K., Hetland, O. & Stormer, F. C. (1971) Eur. J. Biochem, 18, 116 - 119]更快、更温和且更高效。用此方法获得的电泳纯制剂进行的实验表明，该酶（a）通过可逆还原相应L-α-羟基羰基的氧代基团产生L-二醇，还能还原不带电荷的α-二羰基的氧代基团，将其转化为L-α-羟基羰基；（b）对NAD具有特异性。这是一种新酶，我们建议将其系统命名为L-二醇：NAD⁺氧化还原酶，推荐名称为L-二醇脱氢酶（NAD）。本文还描述了该酶的分子量、pI、对底物的亲和力和pH曲线。