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Information on EC 4.5.1.2 - 3-chloro-D-alanine dehydrochlorinase
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4.5.1.2 3-chloro-D-alanine dehydrochlorinaseIUBMB Comments
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.
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Word Map
- 4.5.1.2
- putida
-
beta-replacement
- cr
- d-cysteine
-
beta-elimination
-
maxima
- desulfhydrase
-
holoenzyme
- phenylhydrazine
-
chlorine
- thioglycolate
- agarose
-
apoenzyme
- ammonia
The enzyme appears in viruses and cellular organisms
Synonyms
3-chloro-d-alanine chloride-lyase, 3-chloro-d-alanine dehydrochlorinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-chloro-D-alanine chloride-lyase
-
-
-
-
beta-chloro-D-alanine dehydrochlorinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-chloro-D-alanine + H2O = pyruvate + chloride + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
beta-replacement
elimination
elimination
-
-
of HCl, C-Cl bond cleavage
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elimination
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alpha,beta elimination
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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.
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CAS REGISTRY NUMBER
COMMENTARY
78990-65-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-chloro-D-alanine + H2O
pyruvate + chloride + NH3
-
-
-
-
?
3-chloro-D-alanine + 2-mercaptoethanol
S-(2-hydroxyethyl)-D-cysteine
-
-
-
?
3-chloro-D-alanine + 2-mercaptoethanol
S-(2-hydroxyethyl)-D-cysteine
-
-
-
?
3-chloro-D-alanine + alpha-thiolglycerol
S-(2,3-dihydroxypropyl)-D-cysteine
-
-
-
?
3-chloro-D-alanine + alpha-thiolglycerol
S-(2,3-dihydroxypropyl)-D-cysteine
-
-
-
?
3-chloro-D-alanine + ethyl thioglycolate
S-(ethoxy-carbonyl-methyl)-D-cysteine
-
-
-
ir
3-chloro-D-alanine + ethyl thioglycolate
S-(ethoxy-carbonyl-methyl)-D-cysteine
-
-
-
ir
3-chloro-D-alanine + ethyl-mercaptane
S-ethyl-D-cysteine
-
-
-
?
3-chloro-D-alanine + methyl-mercaptane
S-methyl-D-cysteine
-
-
-
?
3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
-
-
-
?
3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
-
-
-
?
3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
-
-
-
?
additional information
?
-
-
specific for 3-chloro-D-alanine
-
?
additional information
?
-
-
the enzyme mainly catalyzes the degradation of D-cysteine to sulfide, NH3, and pyruvate, EC 4.4.1.15. D-Ser is a poor substrate while the enzyme is inactive with respect to L-Ser and 1-amino-1-carboxy cyclopropane, substrate specificity and ligand binding structures, detailed overview. Ser78 and Gln77 are key determinants of enzyme specificity
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-chloro-D-alanine + H2O
pyruvate + chloride + NH3
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a fold type II pyridoxal 5'-phosphate-dependent enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.84
beta-Chloro-D-alanine
-
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
the polypeptide fold of the enzyme consists of a small domain (residues 48-161) and a large domain (residues 1-47 and 162-328)
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H80Q
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Q77H
-
site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 30% activity with beta-chloro-D-alanine
S78A
-
site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 20% activity with beta-chloro-D-alanine
T288E
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
T315L/T288E
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Y261F
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Y287F
-
site-directed mutagenesis, inactive mutant with all substrates tested
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamada, H.; Nagasawa, T.; Ohkishi, H.; Kawakami, B.; Tani, Y.
Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida
Biochem. Biophys. Res. Commun.
100
1104-1110
1981
Pseudomonas putida, Pseudomonas putida CR1-1
brenda
Nagasawa, T.; Hosono, H.; Ohkishi, H.; Yamada, H.
Synthesis of S-(carboxymethyl)-D-cysteine by 3-chloro-D-alanine chloride-lyase of pseudomonas putida CR 1-1
Appl. Biochem. Biotechnol.
8
481-489
1983
Pseudomonas putida, Pseudomonas putida CR1-1
brenda
Soda, K.
Synthesis of D-cysteine by a new pyridoxal enzyme
Trends Biochem. Sci.
8
152-153
1983
Pseudomonas putida, Pseudomonas putida CR1-1
-
brenda
Nagasawa, T.; Hosano, H.; Ohkishi, H.; Tani, Y.; Yamada, H.
Synthesis of D-cysteine-related amino acids by 3-chloro-D-alanine chloride-lyase of Pseudomonas putida CR 1-1
Biochem. Biophys. Res. Commun.
111
809-816
1983
Pseudomonas putida, Pseudomonas putida CR1-1
brenda
Nagasawa, T.; Hosano, H.; Yamano, H.; Ohkishi, H.; Tani, Y.; Yamada, H.
Synthesis of C-cysteine from a racemate of 3-chloroalanine by phenylhydrazine-treated cells of Pseudomonas putida CR 1-1
Agric. Biol. Chem.
47
861-868
1983
Pseudomonas putida, Pseudomonas putida CR1-1
-
brenda
Nagasawa, T.; Yamano, H.; Hosono, H.; Yamada, H.; Ohkishi, H.; Tani, Y.
Enzymatic synthesis of D-cysteine by 3-chloro-D-alanine resistant Pseudomonas putida CR 1-1
Agric. Biol. Chem.
46
3003-3010
1982
Pseudomonas putida, Pseudomonas putida CR1-1
-
brenda
Nagasawa, T.; Ohkishi, H.; Kavakami, B.; Yamano, H.; Hosono, H.; Tani, Y.; Yamada, H.
3-Chloro-D-alanine chloride-lyase (deaminating) of Pseudomonas putida CR 1.1. Purification and characterization of a novel enzyme occurring in 3-chloro-D-alanine-resistant pseudomonads
J. Biol. Chem.
257
13749-13756
1982
Pseudomonas putida
brenda
Nagasawa, T.; Ishii, T.; Yamada, H.
Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1
Arch. Microbiol.
149
413-416
1988
Pseudomonas putida
brenda
Nagasawa, T.; Ohkishi, H.; Yamada, H.
3-Chloro-D-alanine chloride-lyase (deaminating) of Pseudomonas putida CR 1-1
Prog. Clin. Biol. Res.
144A
365-375
1984
Pseudomonas putida
brenda
Bharath, S.R.; Bisht, S.; Harijan, R.K.; Savithri, H.S.; Murthy, M.R.
Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase
PLoS ONE
7
e36267
2012
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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