BRENDA home
History
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.
EC Tree
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, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(L-SOS) lyase
-
-
-
-
ammonia-lyase, serine sulfate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-serine O-sulfate + H2O = pyruvate + NH3 + sulfate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of NH3, C-N bond cleavage
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-serine-O-sulfate ammonia-lyase (pyruvate-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9054-70-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
-
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
-
?
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
-
-
?
additional information
?
-
-
aminoacrylate is an intermediate in the enzyme-catalysed degradation of L-serine O-sulfate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
4 mM: 53% inhibition, 10 mM: 96% inhibition; potent non-competitive
O-phospho-L-serine
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, Vigna radiata var. radiata, Pisum sativum, Raphanus sativus
-
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.3.1.10)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda4 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)