A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity.
The genome sequence of Streptomyces coelicolor A3(2) contains 51 putative lipase and esterase genes mostly of unknown function. The gene estB (locus SCO 6966) was expressed as a His-tagged protein in E. coli. Esterase B was active at low temperatures exerting its maximum activity at 30 degrees C and retaining more than 25% of its activity at 4 degrees C. The optimum pH was 8-8.5. The enzyme was active against short synthetic p-nitrophenylesters (C2-C10) with maximum activity towards the acetate ester (C2). The esterase was tested on 13 series of racemic esters of potential interest for the synthesis of chiral pharmaceutical compounds. 4 of the series were substrates and a modest degree of enantioselectivity was observed (enantiomeric ratios of 1.1-1.9).
Soror
Sameh H
SH
LB Genetik University of Kaiserslautern, Postfach 3049, 67653 Kaiserslautern, Germany.
Verma
V
V
Rao
Ren
R
Rasool
Shafaq
S
Koul
S
S
Qazi
G N
GN
Cullum
John
J
D000085:Acetates / Q000378:metabolism*; D003080:Cold Temperature; D004269:DNA, Bacterial / Q000235:genetics; D004795:Enzyme Stability; D004950:Esterases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D016680:Genome, Bacterial; D006863:Hydrogen-Ion Concentration; D013237:Stereoisomerism; D048372:Streptomyces coelicolor / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D000085:Acetates; D004269:DNA, Bacterial; D004950:Esterases