1vgc
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GAMMA-CHYMOTRYPSIN L-PARA-CHLORO-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
OverviewOverview
In order to probe the structural basis of stereoselectivity in the serine, protease family, a series of enantiomeric boronic acids, RCH2CH(NHCOCH3)B(OH)2 has been synthesized and kinetically characterized, as transition-state analog inhibitors using alpha-chymotrypsin and, subtilisin Carlsberg as model systems. When the R-substituent in this, series was changed from a p-chlorophenyl to a 1-naphthyl group, alpha-chymotrypsin, but not subtilisin, reversed its usual preference for, l-enantiomers and bound more tightly to the D-enantiomer [Martichonok, V., & Jones, J. B. (1996) J. Am. Chem. Soc. 118, 950-958]. The structural, factors responsible for the differences in stereoselectivity between the, two enzymes have been explored by X-ray crystallographic examination of, subtilisin ... [(full description)]
About this StructureAbout this Structure
1VGC is a [Protein complex] structure of sequences from [Bos taurus] with SO4 and V36 as [ligands]. Active as [[1]], with EC number [3.4.21.1]. Full crystallographic information is available from [OCA].
ReferenceReference
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:9425066
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