Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity.
Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Jinming
J
Ma
Qianda
Q
Lu
Ye
Y
Yuan
Honghua
H
Ge
Kuai
K
Li
Wei
W
Zhao
Yongxiang
Y
Gao
Liwen
L
Niu
Maikun
M
Teng
D000595:Amino Acid Sequence; D002265:Carboxylic Ester Hydrolases / Q000096:biosynthesis / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D057075:Enzyme Assays; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis / Q000737:chemistry*; D016415:Sequence Alignment; D040681:Structural Homology, Protein
D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; C115452:IAH1 protein, S cerevisiae; D002265:Carboxylic Ester Hydrolases