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Information on EC 4.3.1.10 - serine-sulfate ammonia-lyase for references in articles please use BRENDA:EC4.3.1.10Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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serine-sulfate ammonia-lyase
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L-serine O-sulfate + H2O = pyruvate + NH3 + sulfate
L-serine O-sulfate + H2O = pyruvate + NH3 + sulfate
mechanism
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L-serine O-sulfate + H2O = pyruvate + NH3 + sulfate
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elimination
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of NH3, C-N bond cleavage
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L-serine-O-sulfate ammonia-lyase (pyruvate-forming)
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ammonia-lyase, serine sulfate
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FR
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FR
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M.R.C. hooded rat
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male M.R.C. hooded rat
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3-chloro-L-alanine methyl ester
?
3-cyano-L-alanine
?
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beta-ureido-alpha-aminopropionic acid
?
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D-cystathionine
?
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D-serine-O-sulfate
pyruvate + NH3 + SO42-
DL-lanthionine
?
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L-cystathionine + H2O
?
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L-serine O-sulfate
pyruvate + NH3 + sulfate
L-seryl-glycine O-sulfate
?
L-seryl-L-alanine O-sulfate
?
L-seryl-L-leucine O-sulfate
?
L-seryl-L-phenylalanine O-sulfate
?
L-seryl-L-valine O-sulfate
?
L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
O-acetyl-L-serine
?
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O-benzyl DL-serine
?
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O-benzyl-L-serine
?
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O-diazoacetyl-L-serine
?
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O-methyl DL-serine
?
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O-succinyl-L-serine
?
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S-benzyl-L-cysteine
?
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S-carbamoyl-L-cysteine
?
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S-ethyl-L-cysteine
?
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S-methyl L-cysteine
?
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S-methyl-L-cysteine
?
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growth pattern is similar to that observed with L-serine O-sulfate
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S-sulfo-L-cysteine
?
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additional information
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3-chloro-L-alanine methyl ester
?
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3-chloro-L-alanine
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3-chloro-L-alanine methyl ester
?
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3-chloro-L-alanine
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3-chloro-L-alanine methyl ester
?
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beta-chloroalanine
?
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beta-chloroalanine
?
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beta-chloro-L-alanine
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D-serine-O-sulfate
pyruvate + NH3 + SO42-
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D-serine-O-sulfate
pyruvate + NH3 + SO42-
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D-serine-O-sulfate
pyruvate + NH3 + SO42-
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activity: 1/40 that towards L-isomer
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
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biosynthesis of cysteine derivates
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L-serine O-sulfate
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biosynthesis of cysteine derivates
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L-serine O-sulfate
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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optimum concentration 188 mM
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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optimum activity at a concentration of 0.05 M
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L-serine O-sulfate
pyruvate + NH3 + sulfate
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quite specific
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L-seryl-glycine O-sulfate
?
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L-seryl-glycine O-sulfate
?
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not very efficient substrate
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L-seryl-L-alanine O-sulfate
?
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L-seryl-L-alanine O-sulfate
?
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not very efficient substrate
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L-seryl-L-leucine O-sulfate
?
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L-seryl-L-leucine O-sulfate
?
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not very efficient substrate
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L-seryl-L-phenylalanine O-sulfate
?
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L-seryl-L-phenylalanine O-sulfate
?
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not very efficient substrate
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L-seryl-L-valine O-sulfate
?
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L-seryl-L-valine O-sulfate
?
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not very efficient substrate
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L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
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activity: 1/30 that towards L-serine O-sulfate
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L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
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L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
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L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
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L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
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weak activity
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additional information
?
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multi-substrate activity of the enzymes A and B with the enzyme A having a preferential activity for L-isomers and enzyme B for D-isomers
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additional information
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Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
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additional information
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multi-substrate activity of the enzymes A and B with the enzyme A having a preferential activity for L-isomers and enzyme B for D-isomers
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additional information
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Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
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additional information
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factors affecting the leavels of th L-serine O-sulfate-degrading system
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additional information
?
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aminoacrylate is an intermediate in the enzyme-catalysed degradation of L-serine O-sulfate
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S-methyl-L-cysteine
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growth pattern is similar to that observed with L-serine O-sulfate
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additional information
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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L-serine O-sulfate
?
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biosynthesis of cysteine derivates
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additional information
?
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Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
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additional information
?
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Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
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additional information
?
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factors affecting the leavels of th L-serine O-sulfate-degrading system
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additional information
?
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aminoacrylate is an intermediate in the enzyme-catalysed degradation of L-serine O-sulfate
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3-Cyano-L-alanine
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10 mM, 36% inhibition and 20 mM, 50% inhibition
4-iodoacetamidosalicylic acid
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irreversible
5-aminoisophthallic acid
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50 mM, 19% inhibition
5-bromo-2-furoic acid
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10 mM, 50% inhibition
aminomalonic acid
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10 mM, 44% inhibition
Benzoic acid
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34 mM, 63% inhibition
cyanide
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1.25 mM, complete inhibition
D-glycerate sulfate
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50 mM, 25% inhibition
D-phospho-L-serine
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weak competitive
DL-homocysteic acid
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50 mM, 21% inhibition; 50 mM, 23% inhibition
hydrazine
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25 mM, complete inhibition
hydrazine hydrochloride
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1 mM: 15% inhibition
hydroxybutyric acid sulfonate
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50 mM, 23% inhibition
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Hydroxylamine hydrochloride
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0.1 mM: 8% inhibition, 1 mM: 13% inhibiotion
Isophthalic acid
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10 mM, 42% inhibition
L-aspartic acid
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40 mM, 20% inhibition
L-cysteic acid
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50 mM, 25% inhibition
L-cysteine S-sulfate
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50 mM, 30% inhibition
L-Glutamic acid
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40 mM, 23% inhibition
L-glycerate sulfate
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40 mM, 42% inhibition
lactic acid sulfonate
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50 mM, 25% inhibition
m-chlorobenzoate
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12.5 mM, 85% inhibition
m-Hydroxybenzoate
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20 mM, 47% inhibition
m-Iodobenzoate
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6.0 mM, 90% inhibition
m-toluic acid
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25 mM, 59% inhibition
pyridoxal 5'-phosphate
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0.06 mg/l, 25-30% inhibition
Rose bengal
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non-competitive
succinic acid
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40 mM, 42% inhibition
terephthalic acid
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50 mM, 53% inhibition
trimesic acid
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50 mM, 19% inhibition
D-serine O-sulfate
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D-serine O-sulfate
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10 mM: 19% inhibition
DL-homoserine O-sulfate
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weak competitive
DL-homoserine O-sulfate
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10 mM: 11% inhibition
hydroxylamine
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25 mM, complete inhibition
iodoacetic acid
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iodoacetic acid
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0.01 mM: 17% inhibition, 0.1 mM: 76% inhibition, 1 mM: 95% inhibition
O-acetyl-L-serine
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potent non-competitive
O-acetyl-L-serine
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4 mM: 53% inhibition, 10 mM: 96% inhibition; potent non-competitive
O-phospho-L-serine
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weak non-competitive
O-phospho-L-serine
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potent non-competitive
O-phospho-L-serine
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5 mM: 44% inhibition, 10 mM: 98% inhibition; potent non-competitive
O-phospho-L-serine
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weak non-competitive
p-chloromercuribenzoate
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at a concentration of 0.1 mM, partly reversible with 2-mercaptoethanol
p-chloromercuribenzoate
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0.01 mM: 18% inhibition, 0.1 mM: 61% inhibition, 1 mM. 94% inhibition
additional information
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additional information
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additional information
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50
3-chloro-L-alanine methyl ester
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2.2
D-cystathionine
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enzyme B
0.17
D-Cystine
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enzyme B
0.14
D-serine O-sulfate
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enzyme B
8.5 - 9.1
L-cystathionine
2.3 - 26
L-serine O-sulfate
20
O-acetyl-L-serine
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enzyme A
2
O-benzyl-DL-serine
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enzyme B, calculated on the basis of the non-reactivity of the L-isomer
1.3
O-benzyl-L-serine
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enzyme A
1.1
S-Benzyl-L-cysteine
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enzyme A
38
S-ethyl-L-cysteine
-
enzyme A
17.8 - 56
S-methyl-L-cysteine
8.5
L-cystathionine
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enzyme B
9.1
L-cystathionine
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enzyme A
2.3
L-serine O-sulfate
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5.4
L-serine O-sulfate
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enzyme B
7.9
L-serine O-sulfate
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enzyme A
23
L-serine O-sulfate
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-
26
L-serine O-sulfate
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alpha enzyme; beta enzyme
17.8
S-methyl-L-cysteine
-
enzyme A
56
S-methyl-L-cysteine
-
enzyme B
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additional information
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additional information
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additional information
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additional information
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7
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in 0.1 M Tris-HCl
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8.5 - 10
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about 65% of the maximal activity at pH 8.5 and about 35% of maximal activity at pH 10.0 in Tris-HCl buffer
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37
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enzyme assay at
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brenda
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50000
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gel filtration, beta enzyme
52000
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gel filtration, alpha enzyme
53800
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high-speed membrane osmometry, alpha enzyme
54500
-
high-speed membrane osmometry, beta enzyme
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4.5 - 8
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stable between
6034
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50
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enzyme B, after 15 min, 30% of the starting activity towards L-serine O-sulfate, 32% towards O-benzyl-DL-serine and 38% towards L-cystathionine. Enzyme A, after 15 min, 71% of the starting activity towards L-serine O-sulfate, 75% towards O-benzyl-DL-serine and 71% towards L-cystathionine
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complete loss of activity if enzyme-containing solution is frozen and thawed
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photooxidation in the presence of Rose Bengal leads to a rapid inactivation
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6033
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-20°C, stable for several weeks
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0°C, for 25 h, remaining activity of 84%
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4°C, 10% loss of activity after 1 week
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Murakoshi, I.; Sanda, A.; Haginiwa, J.
L-Serine O-sulphate lyase, a new enzyme in extracts from higher plants
Chem. Pharm. Bull.
25
1829-1832
1977
Allium cepa, Allium sativum, Brassica rapa subsp. oleifera, Citrullus lanatus subsp. vulgaris, Fagopyrum esculentum, Leucaena leucocephala, Mimosa pudica, Pisum sativum, Raphanus sativus, Vigna radiata var. radiata
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brenda
Tudball, N.; Thomas, P.
Studies on the inhibition of the L-serine O-sulphate-degrading system of pig liver and the topography of its active site
Eur. J. Biochem.
40
25-29
1973
Sus scrofa
brenda
Tudball, N.; Thomas, P.
The enzyme degradation of L-serine O-sulphate. Mechanism of the reaction
Biochem. J.
128
41-46
1972
Sus scrofa
brenda
Tudball, N.; Thomas, J.H.
L-Serine O-sulphate-degrading system of rat liver
Methods Enzymol.
17B
361-367
1971
Rattus norvegicus
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brenda
Tudball, N.; O'Neill, J.G.
Substrate specificity of the L-serine O-sulphate degrading activities of Pseudomonas FR
Biochim. Biophys. Acta
429
616-623
1976
Pseudomonas sp., Pseudomonas sp. FR
brenda
Tudball, N.; Thomas, P.; Fowler, J.A.
Factors affecting the levels of the L-serine O-sulphate-degrading system of rat liver
Biochim. Biophys. Acta
338
83-91
1974
Rattus norvegicus
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brenda
Tudball, N.; Thomas, P.
The enzymic degradation of L-serine O-sulphate by a specific system from pig liver
Biochem. J.
126
187-191
1972
Sus scrofa
brenda
Tudball, N.; Thomas, P.; Bailey-Wood, R.
The purification and properties of the L-serine O-sulphate degrading system of pig liver
Biochem. J.
121
747-752
1971
Sus scrofa
brenda
Thomas, J.H.; Tudball, N.
Studies on the enzymic degradation of L-serine O-sulphate by a rat liver preparation
Biochem. J.
105
467-472
1967
Rattus norvegicus
brenda
Tudball, N.; Thomas, P.
Short communications. The enzymic and non-enzymic cleavage of N-terminal L-serine O-sulphate
Biochem. J.
120
895-897
1970
Sus scrofa
brenda
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