Literature summary for 4.5.1.2 extracted from

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 (2012), PLoS ONE, 7, e36267.

Search for more literature for 4.5.1.2

Cloned(Commentary)

Cloned (Comment)	Organism
epression of His6-tagged enzyme in Escherichia coli	Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

Protein Variants	Comment	Organism
H80Q	site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme	Salmonella enterica subsp. enterica serovar Typhimurium
Q77H	site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 30% activity with beta-chloro-D-alanine	Salmonella enterica subsp. enterica serovar Typhimurium
S78A	site-directed mutagenesis, the mutant is inactive with respect to D-Cys, but retains significant 20% activity with beta-chloro-D-alanine	Salmonella enterica subsp. enterica serovar Typhimurium
T288E	site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme	Salmonella enterica subsp. enterica serovar Typhimurium
T315L/T288E	site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme	Salmonella enterica subsp. enterica serovar Typhimurium
Y261F	site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme	Salmonella enterica subsp. enterica serovar Typhimurium
Y287F	site-directed mutagenesis, inactive mutant with all substrates tested	Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.84	-	beta-Chloro-D-alanine	recombinant His6-tagged enzyme, pH and temperature not specified in the publication	Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
beta-chloro-D-alanine + H2O	Salmonella enterica subsp. enterica serovar Typhimurium	-	pyruvate + chloride + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography	Salmonella enterica subsp. enterica serovar Typhimurium

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-chloro-D-alanine + H2O	-	Salmonella enterica subsp. enterica serovar Typhimurium	pyruvate + chloride + NH3	-	?
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	Salmonella enterica subsp. enterica serovar Typhimurium	?	-	?

Subunits

Subunits	Comment	Organism
More	the polypeptide fold of the enzyme consists of a small domain (residues 48-161) and a large domain (residues 1-47 and 162-328)	Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

Synonyms	Comment	Organism
DCyD	-	Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	a fold type II pyridoxal 5'-phosphate-dependent enzyme	Salmonella enterica subsp. enterica serovar Typhimurium

General Information

General Information	Comment	Organism
evolution	the enzyme structurally belongs to the fold type II pyridoxal 5'-phosphate-dependent enzyme family	Salmonella enterica subsp. enterica serovar Typhimurium
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	Salmonella enterica subsp. enterica serovar Typhimurium

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)