Information on EC 4.5.1.2 - 3-chloro-D-alanine dehydrochlorinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.5.1.2
-
RECOMMENDED NAME
GeneOntology No.
3-chloro-D-alanine dehydrochlorinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-chloro-D-alanine + H2O = pyruvate + chloride + NH3
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-replacement
elimination
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alpha,beta elimination; of HCl, C-Cl bond cleavage
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SYSTEMATIC NAME
IUBMB Comments
3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-chlorine bond, releasing a chloride and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme's activity can also result in beta-replacement reactions, e.g. in the presence of hydrogen sulfide it can convert 3-chloro-D-alanine into D-cysteine and chloride.
CAS REGISTRY NUMBER
COMMENTARY hide
78990-65-5
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme structurally belongs to the fold type II pyridoxal 5'-phosphate-dependent enzyme family
additional information
-
active site structure analysis and comparisons, residue Tr287 is important for catalysis, while His80 and Tyr261 may not be directly involved in the degradation of beta-chloro-D-alanine, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-chloro-D-alanine + 2-mercaptoethanol
S-(2-hydroxyethyl)-D-cysteine
show the reaction diagram
3-chloro-D-alanine + allyl mercaptane
S-allyl-D-cysteine
show the reaction diagram
3-chloro-D-alanine + alpha-thiolglycerol
S-(2,3-dihydroxypropyl)-D-cysteine
show the reaction diagram
3-chloro-D-alanine + benzyl-mercaptane
S-benzyl-D-cysteine
show the reaction diagram
-
-
-
?
3-chloro-D-alanine + ethyl thioglycolate
S-(ethoxy-carbonyl-methyl)-D-cysteine
show the reaction diagram
3-chloro-D-alanine + ethyl-mercaptane
S-ethyl-D-cysteine
show the reaction diagram
3-chloro-D-alanine + H2O
?
show the reaction diagram
3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
show the reaction diagram
3-chloro-D-alanine + H2S
D-cysteine + HCl
show the reaction diagram
3-chloro-D-alanine + methyl-mercaptane
S-methyl-D-cysteine
show the reaction diagram
3-chloro-D-alanine + n-butyl-mercaptane
S-n-butyl-D-cysteine
show the reaction diagram
3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
show the reaction diagram
3-chloro-D-alanine + NaHS
D-cysteine + NaCl
show the reaction diagram
3-chloro-D-alanine + phenyl-mercaptane
S-phenyl-D-cysteine
show the reaction diagram
beta-chloro-D-alanine + H2O
pyruvate + chloride + NH3
show the reaction diagram
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-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-chloro-D-alanine + H2O
?
show the reaction diagram
beta-chloro-D-alanine + H2O
pyruvate + chloride + NH3
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-chloro-L-alanine
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competitive
cycloserine
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cysteamine dihydrochloride
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D-penicillamine
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hydroxylamine HCl
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iodoacetate
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L-Penicillamine
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phenylhydrazine
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Semicarbazide hydrochloride
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thiol reagents
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061 - 8.1
3-chloro-D-alanine
0.84
beta-Chloro-D-alanine
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recombinant His6-tagged enzyme, pH and temperature not specified in the publication
0.18
D-Cysteine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
311
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alpha,beta elimination
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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D-cysteine synthesis
8.5
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cysteine synthesis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
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2 * 38000, SDS-PAGE
76000
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sedimentation equilibrium
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the polypeptide fold of the enzyme consists of a small domain (residues 48-161) and a large domain (residues 1-47 and 162-328)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with D-Cys, beta-chloro-D-alanine, 1-amino-1-carboxy cyclopropane, D-Ser, L-Ser, D-cycloserine, and L-cycloserine, X-ray diffraction structure determination and analysis at 1.7-2.6 A resolution, modeling
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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34751
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
15 min stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
several months at -20C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
epression of His6-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H80Q
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site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Q77H
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site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 30% activity with beta-chloro-D-alanine
S78A
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site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 20% activity with beta-chloro-D-alanine
T288E
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site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
T315L/T288E
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site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Y261F
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site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Y287F
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site-directed mutagenesis, inactive mutant with all substrates tested