期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 10, 期 3, 页码 545-550出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0968-0896(01)00307-8
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资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM057179] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM 57179, GM 55387] Funding Source: Medline
The Thermotoga maritima aldolase gene has been cloned into a T7 expression vector and overexpressed in Escherichia coli. The preparation yields 470 UL-1 of enzyme at a specific activity of 9.4 U mg(-1). During retroaldol cleavage of KDPG, the enzyme shows a k(cat) that decreases with decreasing temperature. A more than offsetting decrease in K-m yields an enzyme that is more efficient at 40 degreesC than at 70 degreesC. The substrate specificity of the enzyme was evaluated in the synthetic direction with a range of aldehyde substrates. Although the protein shows considerable structural homology to KDPG aldolases from mesophilic sources, significant differences in substrate specificity exist. A preparative scale reaction between 2-pyridine carboxaldehyde and pyruvate provided product of the same absolute configuration as mesophilic enzymes, but with diminished stereoselectivity. (C) 2002 Elsevier Science Ltd. All rights reserved.
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