Studies on structure-function relationships of acetolactate decarboxylase from Enterobacter cloacae.

ABSTRACT: Acetoin is an important bio-based platform chemical with wide applications. Among all bacterial strains, Enterobacter cloacae is a well-known acetoin producer via α-acetolactate decarboxylase (ALDC), which converts α-acetolactate into acetoin and is identified as the key enzyme in the biosynthetic pathway of acetoin. In this work, the enzyme properties of Enterobacter cloacae ALDC (E.c.-ALDC) were characterized, revealing a K _m value of 12.19 mM and a k _cat value of 0.96 s^-1. Meanwhile, the optimum pH of E.c.-ALDC was 6.5, and the activity of E.c.-ALDC was activated by Mn²⁺, Ba²⁺, Mg²⁺, Zn²⁺ and Ca²⁺, while Cu²⁺ and Fe²⁺ signi

SUBMITTER: Ji F 

PROVIDER: S-EPMC9090609 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature