4.4.1.28: L-cysteine desulfidase
This is an abbreviated version!
For detailed information about L-cysteine desulfidase, go to the full flat file.
Reaction
Synonyms
aecD, At5g28030, CDL, CFL1_01513, cystalysin, DES1, L-cysteine desulfhydrase, les, MJ1025
ECTree
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Substrates Products
Substrates Products on EC 4.4.1.28 - L-cysteine desulfidase
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REACTION DIAGRAM
S-(2-methyl-4-oxopentan-2-yl)-L-cysteine + H2O
NH3 + pyruvate + 4-methyl-4-sulfanylpentan-2-one
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-
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?
NH3 + pyruvate + homocysteine
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-
-
?
L-cystathionine + H2O
NH3 + pyruvate + homocysteine
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-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
hydrogen sulfide generated by L-cysteine desulfhydrase acts upstream of nitric oxide to modulate abscisic acid-dependent stomatal closure
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine serves as a poor substrate
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme plays an important role in L-cysteine degradation in Corynebacterium glutamicum cells
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine serves as a poor substrate
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
no activity with DLK-homocysteine, D-cysteine, L-cystine and cystathionine
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
possible involvement in iron-sulfur center biosynthesis
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme is very specific for L-cysteine, with no activity being detected with D-cysteine, L-homocysteine, 3-mercaptopropionic acid (cysteine without the amino group), cysteamine (cysteine without the carboxylic acid), or mercaptolactate (the hydroxyl analogue of cysteine)
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
possible involvement in iron-sulfur center biosynthesis
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
the enzyme is very specific for L-cysteine, with no activity being detected with D-cysteine, L-homocysteine, 3-mercaptopropionic acid (cysteine without the amino group), cysteamine (cysteine without the carboxylic acid), or mercaptolactate (the hydroxyl analogue of cysteine)
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-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
DL-homocysteine, cysteinyl glycine, and glutathione are not substrates to produce hydrogen sulfide
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
DL-homocysteine, cysteinyl glycine, and glutathione are not substrates to produce hydrogen sulfide
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
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the enzyme is responsible for in vivo cysteine catabolism by Treponema denticola
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?
L-cysteine + H2O
sulfide + NH3 + pyruvate
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strong preference for L-cysteine over D-cysteine, H2S production is 483-fold slower with D-cysteine than with L-cysteine. It is far more active towards L-cysteine than towards the other standard amino acids that undergo pyridoxal phosphate-dependent beta-elimination reactions (serine, threonine, tryptophan and tyrosine). The enzyme tolerated small modifications to the carboxylate of L-cysteine (i.e., the methyl and ethyl esters of L-cysteine are good substrates), but the smallest possible peptide with an N-terminal cysteine, L-cysteinylglycine, is a very poor substrate
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?
L-cystine + H2O
?
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?
NH3 + pyruvate + cysteamine
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?
S-aminoethyl-L-cysteine + H2O
NH3 + pyruvate + cysteamine
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-
?
?
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the enzyme shows a clear preference for aminoethyl-L-cysteine together with L-cystine and the non-protein amino acid L-djenkolate. Enzyme additionally acts as cysteine-S-conjugate beta-lyase in vitro, reaction of EC 4.4.1.13, and is able to cleave a cysteinylated substrate precursor into the corresponding thiol. Enzyme has no alpha,gamma-elimination activity towards L-methionine to produce methanethiol
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-
?
additional information
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the enzyme shows a clear preference for aminoethyl-L-cysteine together with L-cystine and the non-protein amino acid L-djenkolate. Enzyme additionally acts as cysteine-S-conjugate beta-lyase in vitro, reaction of EC 4.4.1.13, and is able to cleave a cysteinylated substrate precursor into the corresponding thiol. Enzyme has no alpha,gamma-elimination activity towards L-methionine to produce methanethiol
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?