Mandelate racemase and class-related enzymes

John A. Gerlt; George L. Kenyon; John W. Kozarich; David J. Neidhart; Gregory A. Petsko; Vincent M. Powers

doi:10.1016/0959-440X(92)90209-P

Mandelate racemase and class-related enzymes

John A. Gerlt, George L. Kenyon, John W. Kozarich, David J. Neidhart, Gregory A. Petsko, Vincent M. Powers

Research output: Contribution to journal › Article › peer-review

Abstract

Mandalate racemase and class-related enzymes have attracted much interest as potentially simple models for studying the chemical basis of enzymic catalysis. Recent studies on mandelate racemase have been particularly fruitful, revealing the structural workings of a racemase for the first time.

Original language	English (US)
Pages (from-to)	736-742
Number of pages	7
Journal	Current Opinion in Structural Biology
Volume	2
Issue number	5
DOIs	https://doi.org/10.1016/0959-440X(92)90209-P
State	Published - Oct 1992
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Online availability

10.1016/0959-440X(92)90209-P

Library availability

Discover UIUC Full Text

Cite this

@article{9bd0c512bfd44e72a94e63206a3d30eb,

title = "Mandelate racemase and class-related enzymes",

abstract = "Mandalate racemase and class-related enzymes have attracted much interest as potentially simple models for studying the chemical basis of enzymic catalysis. Recent studies on mandelate racemase have been particularly fruitful, revealing the structural workings of a racemase for the first time.",

author = "Gerlt, {John A.} and Kenyon, {George L.} and Kozarich, {John W.} and Neidhart, {David J.} and Petsko, {Gregory A.} and Powers, {Vincent M.}",

year = "1992",

month = oct,

doi = "10.1016/0959-440X(92)90209-P",

language = "English (US)",

volume = "2",

pages = "736--742",

journal = "Current Opinion in Structural Biology",

issn = "0959-440X",

publisher = "Elsevier Ltd",

number = "5",

}

TY - JOUR

T1 - Mandelate racemase and class-related enzymes

AU - Gerlt, John A.

AU - Kenyon, George L.

AU - Kozarich, John W.

AU - Neidhart, David J.

AU - Petsko, Gregory A.

AU - Powers, Vincent M.

PY - 1992/10

Y1 - 1992/10

N2 - Mandalate racemase and class-related enzymes have attracted much interest as potentially simple models for studying the chemical basis of enzymic catalysis. Recent studies on mandelate racemase have been particularly fruitful, revealing the structural workings of a racemase for the first time.

AB - Mandalate racemase and class-related enzymes have attracted much interest as potentially simple models for studying the chemical basis of enzymic catalysis. Recent studies on mandelate racemase have been particularly fruitful, revealing the structural workings of a racemase for the first time.

UR - http://www.scopus.com/inward/record.url?scp=0000950510&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0000950510&partnerID=8YFLogxK

U2 - 10.1016/0959-440X(92)90209-P

DO - 10.1016/0959-440X(92)90209-P

M3 - Article

AN - SCOPUS:0000950510

SN - 0959-440X

VL - 2

SP - 736

EP - 742

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 5

ER -

Mandelate racemase and class-related enzymes

Abstract

ASJC Scopus subject areas

Online availability

Library availability

Related links

Fingerprint

Cite this