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EC Tree
IUBMB 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.
The enzyme appears in viruses and cellular organisms
Synonyms
3-chloro-d-alanine chloride-lyase, 3-chloro-d-alanine dehydrochlorinase,
more
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3-chloro-D-alanine chloride-lyase
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beta-chloro-D-alanine dehydrochlorinase
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3-chloro-D-alanine + H2O = pyruvate + chloride + NH3
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beta-replacement
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elimination
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of HCl, C-Cl bond cleavage
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elimination
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alpha,beta elimination
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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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3-chloro-D-alanine + 2-mercaptoethanol
S-(2-hydroxyethyl)-D-cysteine
3-chloro-D-alanine + allyl mercaptane
S-allyl-D-cysteine
3-chloro-D-alanine + alpha-thiolglycerol
S-(2,3-dihydroxypropyl)-D-cysteine
3-chloro-D-alanine + benzyl-mercaptane
S-benzyl-D-cysteine
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3-chloro-D-alanine + ethyl thioglycolate
S-(ethoxy-carbonyl-methyl)-D-cysteine
3-chloro-D-alanine + ethyl-mercaptane
S-ethyl-D-cysteine
3-chloro-D-alanine + H2O
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
3-chloro-D-alanine + H2S
D-cysteine + HCl
3-chloro-D-alanine + methyl-mercaptane
S-methyl-D-cysteine
3-chloro-D-alanine + n-butyl-mercaptane
S-n-butyl-D-cysteine
3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
3-chloro-D-alanine + NaHS
D-cysteine + NaCl
3-chloro-D-alanine + phenyl-mercaptane
S-phenyl-D-cysteine
beta-chloro-D-alanine + H2O
pyruvate + chloride + NH3
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additional information
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3-chloro-D-alanine + 2-mercaptoethanol
S-(2-hydroxyethyl)-D-cysteine
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3-chloro-D-alanine + 2-mercaptoethanol
S-(2-hydroxyethyl)-D-cysteine
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3-chloro-D-alanine + allyl mercaptane
S-allyl-D-cysteine
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3-chloro-D-alanine + allyl mercaptane
S-allyl-D-cysteine
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3-chloro-D-alanine + alpha-thiolglycerol
S-(2,3-dihydroxypropyl)-D-cysteine
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3-chloro-D-alanine + alpha-thiolglycerol
S-(2,3-dihydroxypropyl)-D-cysteine
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3-chloro-D-alanine + ethyl thioglycolate
S-(ethoxy-carbonyl-methyl)-D-cysteine
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3-chloro-D-alanine + ethyl thioglycolate
S-(ethoxy-carbonyl-methyl)-D-cysteine
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3-chloro-D-alanine + ethyl-mercaptane
S-ethyl-D-cysteine
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3-chloro-D-alanine + ethyl-mercaptane
S-ethyl-D-cysteine
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3-chloro-D-alanine + ethyl-mercaptane
S-ethyl-D-cysteine
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3-chloro-D-alanine + H2O
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3-chloro-D-alanine + H2O
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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ir
3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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ir
3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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ir
3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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ir
3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2O
pyruvate + HCl + NH3
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3-chloro-D-alanine + H2S
D-cysteine + HCl
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3-chloro-D-alanine + H2S
D-cysteine + HCl
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3-chloro-D-alanine + methyl-mercaptane
S-methyl-D-cysteine
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3-chloro-D-alanine + methyl-mercaptane
S-methyl-D-cysteine
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3-chloro-D-alanine + methyl-mercaptane
S-methyl-D-cysteine
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3-chloro-D-alanine + n-butyl-mercaptane
S-n-butyl-D-cysteine
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3-chloro-D-alanine + n-butyl-mercaptane
S-n-butyl-D-cysteine
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3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
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3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
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3-chloro-D-alanine + n-propyl-mercaptane
S-n-propyl-D-cysteine
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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ir
3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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ir
3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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ir
3-chloro-D-alanine + NaHS
D-cysteine + NaCl
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3-chloro-D-alanine + phenyl-mercaptane
S-phenyl-D-cysteine
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3-chloro-D-alanine + phenyl-mercaptane
S-phenyl-D-cysteine
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additional information
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specific for 3-chloro-D-alanine
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additional information
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specific for 3-chloro-D-alanine
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additional information
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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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3-chloro-D-alanine + H2O
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beta-chloro-D-alanine + H2O
pyruvate + chloride + NH3
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3-chloro-D-alanine + H2O
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3-chloro-D-alanine + H2O
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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2 mol pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
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a fold type II pyridoxal 5'-phosphate-dependent enzyme
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3-chloro-L-alanine
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competitive
cysteamine dihydrochloride
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Semicarbazide hydrochloride
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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
0.061
3-chloro-D-alanine
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8.1
3-chloro-D-alanine
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311
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alpha,beta elimination
additional information
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additional information
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7.5 - 8
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D-cysteine synthesis
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CR1-1
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brenda
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brenda
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brenda
CR1-1
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brenda
CR1-1, AKU 867
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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evolution
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the enzyme structurally belongs to the fold type II pyridoxal 5'-phosphate-dependent enzyme family
additional information
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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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38000
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2 * 38000, SDS-PAGE
76000
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sedimentation equilibrium
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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)
dimer
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2 * 38000, SDS-PAGE
dimer
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2 * 38000, SDS-PAGE
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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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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
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several months at -20°C
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recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
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epression of His6-tagged enzyme in Escherichia coli
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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
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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
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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
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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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