Low-specificity L-threonine aldolase of Pseudomonas sp. NCIMB 10558:: purification, characterization and its application to β-hydroxy-α-amino acid synthesis

被引:19
作者
Liu, JQ
Ito, S
Dairi, T
Itoh, N
Shimizu, S
Yamada, H
机构
[1] Toyama Prefectural Univ, Biotechnol Res Ctr, Lab Biocatalyt Chem, Toyama 93903, Japan
[2] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto, Japan
关键词
D O I
10.1007/s002530051235
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
Low-specificity L-threonine aldolase, catalyzing the reversible cleavage/condensation reaction between L-threonine/L-allo-threonine and glycine plus acetaldehyde, was purified to homogeneity from Pseudomonas sp. NCIMB 10558. The enzyme has an apparent molecular mass of approximately 145 kDa and consists of four identical subunits with a molecular mass of 35 kDa. The enzyme, requiring pyridoxal-5'-phosphate as a coenzyme, is strictly L-specific at the alpha position, whereas it can not distinguish between threo and erythro forms at the beta position. Besides the reversible cleavage/condensation of threonine, the enzyme also catalyzes the reversible interconversion between glycine plus various aldehydes and L-beta-hydroxy-alpha-amino acids, including L-beta-(3,4-dihydroxyphenyl)serine, L-beta-(3,4-methylenedioxyphenyl)serine and L-beta-phenylserine, providing a new route for the industrial production of these important amino acids.
引用
收藏
页码:702 / 708
页数:7
相关论文
共 25 条