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PMID: 7855594 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids.

Science (New York, N.Y.) ·Vol. 267 ·No. 5201 ·1995-02-24 ·Pages 1159-61

Babbitt PC, Mrachko GT, Hasson MS, Huisman GW, Kolter R, Ringe D, Petsko GA, Kenyon GL, Gerlt JA

Abstract

Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. In this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.

MeSH Terms
Amino Acid Sequence Base Sequence Binding Sites Histidine/metabolism Hydro-Lyases/chemistry,genetics,metabolism Intramolecular Lyases Isomerases/chemistry,metabolism Lysine/metabolism Molecular Sequence Data Open Reading Frames Operon Protons Pseudomonas putida/enzymology,genetics Racemases and Epimerases/chemistry,metabolism
Chemicals
Protons Histidine Hydro-Lyases galactonate dehydratase Isomerases Racemases and Epimerases mandelate racemase Intramolecular Lyases muconate cycloisomerase Lysine
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Babbitt P C
Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143.
Mrachko G T
Hasson M S
Huisman G W
Kolter R
Ringe D
Petsko G A
Kenyon G L
Gerlt J A
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1995-02-24
Pages
1159-61
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM-34572 · United States
NIGMS NIH HHS · GM-40570 · United States
Databases
GENBANK
U19577
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