Sequence of HAD_PSEUY
EC Number:3.8.1.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
Other sequences found for EC No. 3.8.1.2
General information:
Sequence
0 MDYIKGIAFD LYGTLFDVHS VVGRCDEAFP GRGREISALW RQKQLEYTWL RSLMNRYVNF
60 QQATEDALRF TCRHLGLDLD ARTRSTLCDA YLRLAPFSEV PDSLRELKRR GLKLAILSNG
120 SPQSIDAVVS HAGLRDGFDH LLSVDPVQVY KPDNRVYELA EQALGLDRSA ILFVSSNAWD
180 ATGARYFGFP TCWINRTGNV FEEMGQTPDW EVTSLRAVVE LFETAAGKAE KG
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
936272
Nardi-Dei V.,Kurihara T.,Okamura T.,Liu J.Q.,Koshikawa H.,Ozaki H.,Terashima Y.,Esaki N.,Soda K.
Comparative studies of genes encoding thermostable L-2-halo acid dehalogenase from Pseudomonas sp. strain YL, other dehalogenases, and two related hypothetical proteins from Escherichia coli.
Appl. Environ. Microbiol.
60
3375-3380
1994
936273
Kurihara T.,Liu J.-Q.,Nardi-Dei V.,Koshikawa H.,Esaki N.,Soda K.
Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues.
J. Biochem.
117
1317-1322
1995
936274
Hisano T.,Hata Y.,Fujii T.,Liu J.-Q.,Kurihara T.,Esaki N.,Soda K.
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold.
J. Biol. Chem.
271
20322-20330
1996
936275
Li Y.F.,Hata Y.,Fujii T.,Hisano T.,Nishihara M.,Kurihara T.,Esaki N.
Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism.
J. Biol. Chem.
273
15035-15044
1998
