Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity

Proteins. 2011 Feb;79(2):662-8. doi: 10.1002/prot.22865.

Authors

Jinming Ma¹, Qianda Lu, Ye Yuan, Honghua Ge, Kuai Li, Wei Zhao, Yongxiang Gao, Liwen Niu, Maikun Teng

Affiliation

¹ Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.

PMID: 21069734
DOI: 10.1002/prot.22865

No abstract available

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Carboxylic Ester Hydrolases / biosynthesis
Carboxylic Ester Hydrolases / chemistry*
Catalytic Domain*
Crystallography, X-Ray
Enzyme Assays
Molecular Sequence Data
Protein Multimerization
Recombinant Fusion Proteins / biosynthesis
Recombinant Fusion Proteins / chemistry*
Saccharomyces cerevisiae / enzymology*
Saccharomyces cerevisiae Proteins / biosynthesis
Saccharomyces cerevisiae Proteins / chemistry*
Sequence Alignment
Structural Homology, Protein

Substances

Recombinant Fusion Proteins
Saccharomyces cerevisiae Proteins
IAH1 protein, S cerevisiae
Carboxylic Ester Hydrolases