Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia coli is a specific α-d-glucose 1-phosphate hydrolase useful for substrate-selective sugar phosphate transformations.

ABSTRACT: Phosphomonoester hydrolases (phosphatases; EC 3.1.3.) often exhibit extremely relaxed substrate specificity which limits their application to substrate-selective biotransformations. In search of a phosphatase catalyst specific for hydrolyzing α-d-glucose 1-phosphate (αGlc 1-P), we selected haloacid dehalogenase-like phosphatase 4 (HAD4) from Escherichia coli and obtained highly active recombinant enzyme through a fusion protein (Z_basic2_HAD4) that contained Z_basic2, a strongly positively charged three α-helical bundle module, at its N-terminus. Highly pure Z_basic2_HAD4 was prepared directly from E. coli cell extract using capture and polishing combined in a single step of cation exchange chromatography. Kinetic studies showed Z_basi

SUBMITTER: Pfeiffer M 

PROVIDER: S-EPMC4251788 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature