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Information on EC 4.3.1.10 - serine-sulfate ammonia-lyase
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4.3.1.10 serine-sulfate ammonia-lyaseSpecify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
(L-SOS) lyase, ammonia-lyase, serine sulfate, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(L-SOS) lyase
-
-
-
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ammonia-lyase, serine sulfate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-serine O-sulfate + H2O = pyruvate + NH3 + sulfate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of NH3, C-N bond cleavage
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SYSTEMATIC NAME
IUBMB Comments
L-serine-O-sulfate ammonia-lyase (pyruvate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9054-70-0
-
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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
S-methyl-L-cysteine
?
-
growth pattern is similar to that observed with L-serine O-sulfate
-
-
-
D-serine-O-sulfate
pyruvate + NH3 + SO42-
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activity: 1/40 that towards L-isomer
-
-
-
L-serine O-sulfate
?
-
biosynthesis of cysteine derivates
-
-
-
L-serine O-sulfate
pyruvate + NH3 + sulfate
-
quite specific
-
-
L-serine O-sulfate
pyruvate + NH3 + sulfate
-
quite specific
-
-
L-serine O-sulfate
pyruvate + NH3 + sulfate
-
optimum concentration 188 mM
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-
L-serine O-sulfate
pyruvate + NH3 + sulfate
-
optimum activity at a concentration of 0.05 M
-
-
-
L-serine O-sulfate
pyruvate + NH3 + sulfate
-
quite specific
-
-
L-threonine O-sulfate
2-oxobutanoate + NH3 + SO42-
-
activity: 1/30 that towards L-serine O-sulfate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
-
-
-
additional information
?
-
-
factors affecting the leavels of th L-serine O-sulfate-degrading system
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-
-
additional information
?
-
-
aminoacrylate is an intermediate in the enzyme-catalysed degradation of L-serine O-sulfate
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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
S-methyl-L-cysteine
?
-
growth pattern is similar to that observed with L-serine O-sulfate
-
-
-
L-serine O-sulfate
?
-
biosynthesis of cysteine derivates
-
-
-
additional information
?
-
-
Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
-
-
-
additional information
?
-
-
Pseudomonas FR posses two distinct L-serine O-sulfate degrading enzymes (A and B)
-
-
-
additional information
?
-
-
factors affecting the leavels of th L-serine O-sulfate-degrading system
-
-
-
additional information
?
-
-
aminoacrylate is an intermediate in the enzyme-catalysed degradation of L-serine O-sulfate
-
-
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetic acid
-
0.01 mM: 17% inhibition, 0.1 mM: 76% inhibition, 1 mM: 95% inhibition
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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5 mM: 44% inhibition, 10 mM: 98% inhibition; potent non-competitive
p-chloromercuribenzoate
-
at a concentration of 0.1 mM, partly reversible with 2-mercaptoethanol
p-chloromercuribenzoate
-
0.01 mM: 18% inhibition, 0.1 mM: 61% inhibition, 1 mM. 94% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
O-benzyl-DL-serine
-
enzyme B, calculated on the basis of the non-reactivity of the L-isomer
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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
8.5 - 10
-
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
-
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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