Abstract
An active site model of the amine:pyruvate aminotransferase (APA) from Vibrio fluvialis JS17 was constructed on the basis of the relationship between substrate structure and reactivity. Due to the broad substrate specificity of the APA, various amino donors (chiral and achiral amine, amino acid, and amino acid derivative) and amino acceptors (keto acid, keto ester, aldehyde, and ketone) were used to explore the active site structure. The result suggested a two-binding site model consisting of two pockets, one large (L) and the other small (S). The difference in the size of each binding pocket and strong repulsion for a carboxylate in the S pocket were key determinants to control its substrate specificity and stereoselectivity. The L pocket showed dual recognition mode for both hydrophobic and carboxyl groups as observed in the side-chain pockets of aspartate aminotransferase and aromatic aminotransferase. Comparison of the model with those of other aminotransferases revealed that the L and S pockets corresponded to carboxylate trap and side-chain pocket, respectively. The active site model successfully explains the observed substrate specificity as well as the stereoselectivity of the APA.
| Original language | English |
|---|---|
| Pages (from-to) | 2848-2853 |
| Number of pages | 6 |
| Journal | Journal of Organic Chemistry |
| Volume | 67 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 2002 May 3 |
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All Science Journal Classification (ASJC) codes
- Organic Chemistry
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Exploring the active site of amine:pyruvate aminotransferase on the basis of the substrate structure-reactivity relationship : How the enzyme controls substrate specificity and stereoselectivity. / shin, jong shik; Kim, Byung Gee.
In: Journal of Organic Chemistry, Vol. 67, No. 9, 03.05.2002, p. 2848-2853.Research output: Contribution to journal › Article
TY - JOUR
T1 - Exploring the active site of amine:pyruvate aminotransferase on the basis of the substrate structure-reactivity relationship
T2 - How the enzyme controls substrate specificity and stereoselectivity
AU - shin, jong shik
AU - Kim, Byung Gee
PY - 2002/5/3
Y1 - 2002/5/3
N2 - An active site model of the amine:pyruvate aminotransferase (APA) from Vibrio fluvialis JS17 was constructed on the basis of the relationship between substrate structure and reactivity. Due to the broad substrate specificity of the APA, various amino donors (chiral and achiral amine, amino acid, and amino acid derivative) and amino acceptors (keto acid, keto ester, aldehyde, and ketone) were used to explore the active site structure. The result suggested a two-binding site model consisting of two pockets, one large (L) and the other small (S). The difference in the size of each binding pocket and strong repulsion for a carboxylate in the S pocket were key determinants to control its substrate specificity and stereoselectivity. The L pocket showed dual recognition mode for both hydrophobic and carboxyl groups as observed in the side-chain pockets of aspartate aminotransferase and aromatic aminotransferase. Comparison of the model with those of other aminotransferases revealed that the L and S pockets corresponded to carboxylate trap and side-chain pocket, respectively. The active site model successfully explains the observed substrate specificity as well as the stereoselectivity of the APA.
AB - An active site model of the amine:pyruvate aminotransferase (APA) from Vibrio fluvialis JS17 was constructed on the basis of the relationship between substrate structure and reactivity. Due to the broad substrate specificity of the APA, various amino donors (chiral and achiral amine, amino acid, and amino acid derivative) and amino acceptors (keto acid, keto ester, aldehyde, and ketone) were used to explore the active site structure. The result suggested a two-binding site model consisting of two pockets, one large (L) and the other small (S). The difference in the size of each binding pocket and strong repulsion for a carboxylate in the S pocket were key determinants to control its substrate specificity and stereoselectivity. The L pocket showed dual recognition mode for both hydrophobic and carboxyl groups as observed in the side-chain pockets of aspartate aminotransferase and aromatic aminotransferase. Comparison of the model with those of other aminotransferases revealed that the L and S pockets corresponded to carboxylate trap and side-chain pocket, respectively. The active site model successfully explains the observed substrate specificity as well as the stereoselectivity of the APA.
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UR - http://www.scopus.com/inward/citedby.url?scp=0037012917&partnerID=8YFLogxK
U2 - 10.1021/jo016115i
DO - 10.1021/jo016115i
M3 - Article
C2 - 11975536
AN - SCOPUS:0037012917
VL - 67
SP - 2848
EP - 2853
JO - Journal of Organic Chemistry
JF - Journal of Organic Chemistry
SN - 0022-3263
IS - 9
ER -