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Information on EC 3.8.1.2 - (S)-2-haloacid dehalogenase and Organism(s) Xanthobacter autotrophicus and UniProt Accession Q60099

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EC Tree
     3 Hydrolases
         3.8 Acting on halide bonds
             3.8.1 In carbon-halide compounds
                3.8.1.2 (S)-2-haloacid dehalogenase
IUBMB Comments
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
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This record set is specific for:
Xanthobacter autotrophicus
UNIPROT: Q60099
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Word Map
The taxonomic range for the selected organisms is: Xanthobacter autotrophicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-haloacid dehalogenase, ph1421, deh99, l-2-dhlb, l-haloacid dehalogenase, (s)-2-haloacid dehalogenase, dehalogenase iva, hadl aj1, l-had, l-dexs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-halo acid dehalogenase
-
-
-
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2-haloacid dehalogenase[ambiguous]
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-
-
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2-haloacid halidohydrolase[ambiguous]
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-
-
-
2-haloalkanoic acid dehalogenase
-
-
-
-
2-haloalkanoid acid halidohydrolase
-
-
-
-
2-halocarboxylic acid dehalogenase II
-
-
-
-
dehalogenase IVa
-
-
-
-
DL-2-haloacid dehalogenase [ambiguous]
-
-
-
-
L-2-haloacid dehalogenase
-
-
-
-
L-DEX
-
-
-
-
L-DEX YL
-
-
-
-
L-DEXs
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-halide hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-2-haloacid halidohydrolase
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
CAS REGISTRY NUMBER
COMMENTARY hide
37289-39-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
show the reaction diagram
-
-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
show the reaction diagram
-
-
-
-
?
1,2-dichloroethane + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-chloropropionate + H2O
D-lactate + HCl
show the reaction diagram
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
-
?
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
?
1,2-dichloroethane + H2O
?
show the reaction diagram
-
-
-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
-
?
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiol reagents
-
not
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HAD_XANAU
253
0
27469
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27430
-
calculated from amino acid sequence
36000
-
gel filtration
38000
-
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and enzyme in intermediate state with substrate L-2-monochloropropionate and monochloroacetate
apoenzyme and enzyme in intermediate state with substrate L-2-monochloropropionate and monochloroacetate
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three-dimensional structure of enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Soda, K.; Kurihara, T.; Liu, J.Q.; Nardi-Dei, V.; Park, C.; Miyagi, M.; Tsunasawa, S.; Esaki, N.
Bacterial 2-haloacid dehalogenases: structures and catalytic properties
Pure Appl. Chem.
68(11)
2097-2103
1996
Xanthobacter autotrophicus, Pseudomonas sp., Rhizobium sp.
-
Manually annotated by BRENDA team
Van der Ploeg, J.; Van Hall, G.; Janssen, D.B.
Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene
J. Bacteriol.
173
7925-7933
1991
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
Manually annotated by BRENDA team
Ridder, I.S.; Rozeboom, H.J.; Kalk, K.H.; Dijkstra, B.W.
Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase
J. Biol. Chem.
274
30672-30678
1999
Xanthobacter autotrophicus (Q60099)
Manually annotated by BRENDA team
Ridder, I.S.; Rozeboom, H.J.; Kalk, K.H.; Janssen, D.B.; Dijkstra, B.W.
Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate
J. Biol. Chem.
272
33015-33022
1997
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
Manually annotated by BRENDA team
Vyazmensky, M.; Geresh, S.
Substrate specificity and product stereochemistry in the dehalogenation of 2-haloacids with the crude enzyme preparation from Pseudomonas putida
Enzyme Microb. Technol.
22
323-328
1998
Xanthobacter autotrophicus, Pseudomonas putida, Pseudomonas putida No. 109
-
Manually annotated by BRENDA team
van der Ploeg, J.; Janssen D.B.
Sequence analysis of the upstream region of dhlB, the gene encoding haloalkanoic acid dehalogease of Xanthobacter autotrophicus GJ10
Biodegradation
6
257-263
1995
Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
Manually annotated by BRENDA team
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
Burkholderia cepacia, Burkholderia cepacia MBA4, Moraxella sp., Moraxella sp. B, Pseudomonas putida, Pseudomonas putida AJ1, Pseudomonas putida No. 109, Pseudomonas sp., Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10
Manually annotated by BRENDA team