Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.8.1.2 - (S)-2-haloacid dehalogenase and Organism(s) Burkholderia cepacia and UniProt Accession Q51645

for references in articles please use BRENDA:EC3.8.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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)]
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Burkholderia cepacia
UNIPROT: Q51645
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Burkholderia cepacia
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, hadl aj1, dehalogenase iva, l-had, 2-halocarboxylic acid dehalogenase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-halo acid dehalogenase
-
-
-
-
2-haloacid dehalogenase[ambiguous]
-
-
-
-
2-haloacid halidohydrolase[ambiguous]
-
-
-
-
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
-
-
-
?
2-chloropropionate + H2O
lactate + HCl
show the reaction diagram
-
-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
?
monobromoacetate + H2O
glycolate + HBr
show the reaction diagram
-
-
-
?
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
-
-
-
?
(S)-2-haloacid + H2O
(R)-2-hydroxyacid + halide
show the reaction diagram
-
-
-
-
?
2-chloropropionate + H2O
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
2-chloropropionate + H2O
lactate + HCl
show the reaction diagram
-
-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
?
monobromoacetate + H2O
glycolate + HBr
show the reaction diagram
-
-
-
?
monochloroacetate + H2O
glycolate + HCl
show the reaction diagram
-
-
-
?
L-2-haloalkanoic acid + H2O
D-2-hydroxyalkanoic acid + halide
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CuSO4
41% inhibition
p-mercuric chlorobenzoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.13
monobromoacetate
pH 7.9, 30°C
additional information
additional information
-
comparison of KM of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
comparison of kcat of wild-type and mutant enzymes
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
the mutation from an acidic to a basic amino acid leads to an alteration in the enzyme pI valiue from 5.1 to 6.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HAD4_BURCE
231
0
25995
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
2 * 27000, SDS-PAGE
58000
gel filtration
25900
-
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 27000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D11E
-
totally inactive in catalysis
D11N
-
totally inactive in catalysis
D11S
-
totally inactive in catalysis
D181N
-
totally inactive in catalysis
N178D
-
defective in catalysis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli and Pseudomonas putida
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsang, J.S.H.; Sam, L.
Cloning and characterization of a cryptic haloacid dehalogenase from Burkholderia cepacia MBA4
J. Bacteriol.
181
6003-6009
1999
Burkholderia cepacia (Q51645)
Manually annotated by BRENDA team
Asmara, W.; Murdiyatmo, U.; Baines, A.J.; Bull, A.T.; Hardman, D.J.
Protein engineering of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4
Biochem. J.
292
69-74
1993
Burkholderia cepacia, Burkholderia cepacia MBA4
-
Manually annotated by BRENDA team
Pang, B.C.M.; Tsang, J.S.H.
Mutagenic analysis of the conserved residues in dehalogenase IVa of Burkholderia cepacia MBA4
FEMS Microbiol. Lett.
204
135-140
2001
Burkholderia cepacia, Burkholderia cepacia MBA4
Manually annotated by BRENDA team
Muridiyatmo, U.; Asmara, W.; Tsang, J.S.H.; Baines, A.J.; Bull, A.T.; Hardmann, D.J.
Molecular biology of the 2-haloacid halidohydrolas IVa from Pseudomonas cepacia MBA4
Biochem. J.
284
87-93
1992
Burkholderia cepacia
-
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