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Information on EC 2.5.1.49 - O-acetylhomoserine aminocarboxypropyltransferase
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EC Tree
2.5.1.49 O-acetylhomoserine aminocarboxypropyltransferaseIUBMB Comments
Also reacts with other thiols and H2S, producing homocysteine or thioethers. The name methionine synthase is more commonly applied to EC 2.1.1.13, methionine synthase. The enzyme from baker's yeast also catalyses the reaction of EC 2.5.1.47 cysteine synthase, but more slowly.
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Word Map
- 2.5.1.49
- cystathionine
- o-acetylserine
- l-methionine
-
4.2.99.10
- o-acetyl-l-serine
-
gamma-lyase
-
gamma-synthase
- l-homocysteine
- o-succinylhomoserine
- o-acetyltransferase
- beta-synthase
-
beta-lyase
- medicine
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
o-acetylhomoserine sulfhydrylase, homocysteine synthase, o-acetyl-l-homoserine sulfhydrylase, gamma-cyano-alpha-aminobutyric acid synthase, oah sulfhydrylase, o-acetylhomoserine sulfhydrolase, o-acetylhomoserine (thiol)-lyase, oah shlase, o-acetylhomoserine aminocarboxypropyltransferase, oah-oas sulfhydrylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AHS
EC 4.2.99.10
gamma-cyano-alpha-aminobutyric acid synthase
MetC
methionine synthase
-
-
-
-
MetY
O-acetyl-L-homoserine (thiol)-lyase
-
-
-
-
O-acetyl-L-homoserine acetate-lyase (adding methanethiol)
-
-
-
-
O-acetyl-L-homoserine sulfhydrolase
-
-
-
-
o-acetyl-L-homoserine sulfhydrylase
O-acetylhomoserine sulfhydrolase
-
-
-
-
O-acetylhomoserine sulfhydrylase
OAH
OAH SHase
OAH SHLase
oah2 gene product
OAHS
Q187D4
EC 4.2.99.10
-
-
formerly
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-homoserine + methanethiol = L-methionine + acetate
Also reacts with other thiols and H2S, producing homocysteine or thioethers. The name methionine synthase is more commonly applied to EC 2.1.1.13 5-methyltetrahydrofolate-homocysteine S-methyltransferase. The enzyme from baker's yeast also catalyses the reaction of EC 2.5.1.47 cysteine synthase, but more slowly
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
gamma-replacement
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase
Also reacts with other thiols and H2S, producing homocysteine or thioethers. The name methionine synthase is more commonly applied to EC 2.1.1.13, methionine synthase. The enzyme from baker's yeast also catalyses the reaction of EC 2.5.1.47 cysteine synthase, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
37290-90-7
-
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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
2 O-acetyl-L-homoserine + dimethyldisulfide
2 L-methionine + 2 acetate
-
dimethyldisulfide may be reductively cleaved into methanethiol prior to assimilation
-
-
?
2 O-acetyl-L-homoserine + H2S
2 L-homocysteine + 2 acetate
-
-
-
-
?
o-acetyl-L-homoserine + KCN
gamma-cyano-alpha-aminobutyric acid + acetate
-
-
-
-
?
O-acetyl-L-homoserine + methanol
O-methyl-homoserine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + n-pentanol
O-pentyl-homoserine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + S2-
L-homocysteine + acetic acid
-
physiological substrate NaHS
-
-
?
O-acetyl-L-serine + methanethiol
?
-
reaction only in phosphate buffer, relative activity compared to O-acetyl-L-homoserine 14.8%
-
-
?
O-acetyl-L-serine + methyl mercaptan
S-methylcysteine + ?
-
-
-
?
O-acetyl-L-serine + S2-
L-cysteine + acetic acid
-
physiological substrate NaHS
-
-
?
O-phosphoryl-L-serine + H2S
L-cysteine + H2O
Q76K51
lesser activity
-
-
?
L-homocysteine + KCN
gamma-cyano-alpha-aminobutyric acid + H2S
-
-
-
-
?
L-homocysteine + KCN
gamma-cyano-alpha-aminobutyric acid + H2S
-
-
-
-
?
L-homoserine + H2S
L-homocysteine + H2O
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q76K51
lesser activity
-
-
?
L-serine + H2S
L-cysteine + H2O
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q76K51
lesser activity
-
-
?
o-acetyl-L-homoserine + CN-
gamma-cyano-alpha-aminobutyric acid + acetate
-
glutamine and glutamic acid synthesis pathway
-
-
?
o-acetyl-L-homoserine + CN-
gamma-cyano-alpha-aminobutyric acid + acetate
-
glutamine and glutamic acid synthesis pathway
-
-
?
O-acetyl-L-homoserine + ethanol
O-ethyl-homoserine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + ethanol
O-ethyl-homoserine + acetic acid
Corynebacterium acetophilum A51
-
-
-
?
O-acetyl-L-homoserine + ethyl mercaptan
L-ethionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + ethyl mercaptan
L-ethionine + acetic acid
-
-
-
?
o-acetyl-L-homoserine + H2S
L-homocysteine + acetate
AY257545
-
-
-
?
o-acetyl-L-homoserine + H2S
L-homocysteine + acetate
AY257545
-
-
-
?
o-acetyl-L-homoserine + H2S
L-homocysteine + acetate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q76K51
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
direct sulfhydrylation pathway, methionine biosynthesis
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
direct sulfhydrylation pathway, biosynthesis of homocysteine
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
direct sulfhydrylation pathway, biosynthesis of homocysteine
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + hydrogen sulfide
L-homocysteine + acetate
-
-
-
?
O-acetyl-L-homoserine + hydrogen sulfide
L-homocysteine + acetate
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
methionine biosynthesis pathway
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
pathway for formation of methionine, incorporation of sulfur, possible temporary function for this enzyme may be formation of methionine from methylmercaptan at times of exhaustion of an exogenous source of sulfur
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
methionine biosynthetic pathway
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetic acid
-
relative activity 100%
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
Corynebacterium acetophilum A51
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methyl mercaptan
L-methionine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methylselenide
seleno-L-methionine + acetic acid
-
-
-
-
?
O-acetyl-L-homoserine + methylselenide
seleno-L-methionine + acetic acid
-
-
-
-
?
O-acetyl-L-homoserine + n-butanol
O-butyl-homoserine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + n-butanol
O-butyl-homoserine + acetic acid
Corynebacterium acetophilum A51
-
-
-
?
O-acetyl-L-homoserine + n-propanol
O-propyl-homoserine + acetic acid
Corynebacterium acetophilum
-
-
-
?
O-acetyl-L-homoserine + n-propanol
O-propyl-homoserine + acetic acid
Corynebacterium acetophilum A51
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q76K51
lesser activity
-
-
?
O-acetyl-L-serine + H2S
L-cysteine + acetic acid
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q93I77
-
-
?
O-succinyl-L-homoserine + H2S
homocysteine + ?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q93I77
-
-
-
?
O-succinyl-L-homoserine + H2S
L-homocysteine + succinate
Q76K51
lesser activity
-
-
?
O-succinyl-L-homoserine + H2S
L-homocysteine + succinate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q76K51
lesser activity
-
-
?
additional information
?
-
Corynebacterium acetophilum
-
O-acetyl-L-serine, L-homoserine, O-succinyl-L-homoserine and O-acetyl-L-threonine are no substrates
-
-
?
additional information
?
-
Corynebacterium acetophilum A51
-
O-acetyl-L-serine, L-homoserine, O-succinyl-L-homoserine and O-acetyl-L-threonine are no substrates
-
-
?
additional information
?
-
-
no cystathione formed from cysteine, no alpha-ketobutyrate formed from O-acetylhomoserine, negligible activity with homoserine and serine, O-succinylhomoserine, O-phosphorylhomoserine, O-acetylserine and O-phosphorylserine are no substrates
-
-
?
additional information
?
-
-
L-homoserine, O-succinyl-DL-homoserine, O-phosphoryl-L-homoserine, L-serine, O-acetyl-L-serine, O-phosphoryl-L-serine react at less than 1% the rate with O-acetyl-L-homoserine
-
-
?
additional information
?
-
-
L-homoserine and O-succinyl-L-homoserine are no substrates
-
-
?
additional information
?
-
-
L-homoserine and O-succinyl-L-homoserine are no substrates
-
-
?
additional information
?
-
-
O-acetyl-L-threonine, O-acetyl-L-tyrosine, O-acetyl-L-hydroxyproline and O-succinyl-DL-homoserine are no substrates
-
-
?
additional information
?
-
-
O-acetyl-L-threonine, O-acetyl-L-tyrosine, O-acetyl-L-hydroxyproline and O-succinyl-DL-homoserine are no substrates
-
-
?
additional information
?
-
-
cystathionine is not synthesized from O-acetylhomoserine and cysteine, O-acetyl-L-serine is no substrate
-
-
?
additional information
?
-
-
the enzyme sulfhydrylates both O-acetyl-L-homoserine and O-acetylserine using sulfide to yield homocysteine and cysteine, respectively
-
-
?
additional information
?
-
-
does not synthesize cystathionine from O-acetyl-L-homoserine and L-cysteine, cannot utilize cysteine as co-substrate in place of H2S, O-acetyl-L-serine, O-acetyl-L-tyrosine, O-acetyl-L-threonine, O-phospho-DL-threonine, O-phospho-L-serine, L-serine-O-sulfate and O-acetyl-L-hydroxyproline are no substrates
-
-
?
additional information
?
-
Q93I77
low cystathione beta-lyase reaction, relative activity 0.12%, no cystathione gamma-lyase reaction
-
-
?
additional information
?
-
-
low cystathione beta-lyase reaction, relative activity 0.12%, no cystathione gamma-lyase reaction
-
-
?
additional information
?
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q93I77
low cystathione beta-lyase reaction, relative activity 0.12%, no cystathione gamma-lyase reaction
-
-
?
additional information
?
-
-
shows with O-acetylserine 1% of the activity with O-acetylhomoserine, no activity with O-succinyl-L-homoserine, homoserine or serine
-
-
?
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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
O-acetyl-L-homoserine + S2-
L-homocysteine + acetic acid
-
physiological substrate NaHS
-
-
?
O-acetyl-L-serine + S2-
L-cysteine + acetic acid
-
physiological substrate NaHS
-
-
?
o-acetyl-L-homoserine + CN-
gamma-cyano-alpha-aminobutyric acid + acetate
-
glutamine and glutamic acid synthesis pathway
-
-
?
o-acetyl-L-homoserine + CN-
gamma-cyano-alpha-aminobutyric acid + acetate
-
glutamine and glutamic acid synthesis pathway
-
-
?
o-acetyl-L-homoserine + H2S
L-homocysteine + acetate
AY257545
-
-
-
?
o-acetyl-L-homoserine + H2S
L-homocysteine + acetate
AY257545
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
Corynebacterium acetophilum
-
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
direct sulfhydrylation pathway, methionine biosynthesis
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
direct sulfhydrylation pathway, biosynthesis of homocysteine
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
direct sulfhydrylation pathway, biosynthesis of homocysteine
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
-
?
O-acetyl-L-homoserine + H2S
L-homocysteine + acetic acid
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
methionine biosynthesis pathway
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
pathway for formation of methionine, incorporation of sulfur, possible temporary function for this enzyme may be formation of methionine from methylmercaptan at times of exhaustion of an exogenous source of sulfur
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
-
-
-
?
O-acetyl-L-homoserine + methanethiol
L-methionine + acetate
-
methionine biosynthetic pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
absolutely required for activity, Km 0.00294 mM
pyridoxal 5'-phosphate
-
only required after enzyme is resolved by dialysis against cysteine
pyridoxal 5'-phosphate
the absorption spectrum of the holoenzyme at pH 7.5 shows a major band in the region of 415-416 nm corresponding to ketoenamine tautomer of the internal aldimines
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
cyanide ions can be replaced as cosubstrates by hydrogen sulfide, methylmercaptan, ethylmercaptan and phenylmercaptan
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl N-[[3-bromo-4-([[2,4-diamino-5-(2,3-dibromopropyl)-5,6,7,8-tetrahydropyrido[3,2-d]pyrimidin-6-yl]methyl]amino)phenyl]carbonyl]glutamate
-
inhibition of methionine synthase, arrest of cell cycle in G1/S phase and apoptosis. Treatment results in increase in cyclin E and cyclin-dependent kinase 2, reduction of caspase-3, poly(ADP-ribose) polymerase, caspase-8, and caspase-9 protein levels
L-propargylglycine
irreversible, rapid inactivation; suicide inhibitor
N-[[3-bromo-4-([[2,4-diamino-5-(2,3-dibromopropyl)-5,6,7,8-tetrahydropyrido[3,2-d]pyrimidin-6-yl]methyl]amino)phenyl]carbonyl]glutamic acid
-
inhibition of methionine synthase, arrest of cell cycle in G1/S phase and apoptosis. Treatment results in increase in cyclin E and cyclin-dependent kinase 2, reduction of caspase-3, poly(ADP-ribose) polymerase, caspase-8, and caspase-9 protein levels
Ngamma-acetyl-L-2,4-diaminobutyric acid
competitive; competitive and reversible inhibition
pyridoxal
-
inhibits the activity competitively with respect to pyridoxal 5'-phosphate
additional information
-
no sulfhydryl reagents inhibits the enzyme, S-adenosylmethionine is no inhibitor
-
additional information
-
no repression by S-adenosyl-L-methionine
-
additional information
-
no end product inhibition by methionine or S-adenosylmethionine observed
-
additional information
-
L-serine, glycine and L-alanine are not inhibitors, dithiothreitol and p-chloromercuribenzoate shows no inhibitory effect
-
additional information
-
p-chloromercuribenzoic acid, 5,5'-dithio-bis(2-nitrobenzoic acid) and monoiodoacetic acid have no inhibitory effect
-
additional information
-
L-serine, glycine, cystathione and S-adenosyl-L-methionine are no inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Expression, purification and preliminary crystallographic analysis of O-acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.6
L-methionine
-
O-acetyl-L-serine sulfhydrylase activity, wild-type and mutant enzymes
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
diethyl N-[[3-bromo-4-([[2,4-diamino-5-(2,3-dibromopropyl)-5,6,7,8-tetrahydropyrido[3,2-d]pyrimidin-6-yl]methyl]amino)phenyl]carbonyl]glutamate
Homo sapiens
-
pH 7.2, 37°C
0.0014
N-[[3-bromo-4-([[2,4-diamino-5-(2,3-dibromopropyl)-5,6,7,8-tetrahydropyrido[3,2-d]pyrimidin-6-yl]methyl]amino)phenyl]carbonyl]glutamic acid
Homo sapiens
-
pH 7.2, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.45
-
mutant strain No. 17, O-acetylhomoserine sulfhydrylase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
7.5
higher activity is shown in potassium phosphate buffer compared to sodium phosphate and Tris-HCl buffers
8
-
optimum for gamma-replacement reaction of O-acetylhomoserine with Na2Se
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
patients with esophageal squamous cell carcinoma, Barretts esophagus-associated esophageal adenocarcinoma, cardiac carcinoma, or gastric carcinoma
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-
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
DDBJ: AB049221, EMBL:AB049221
Q93I77
SwissProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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wild-type cells are able to grow on both methanethiol and dimethyldisulfide as sole sulfur sources. Both sulfur compounds are incorporated as an entire molecule, adding the terminal S-CH3 group to O-acetylhomoserine. In this reaction, methionine is directly formed. the reaction is catalyzed by O-acetylhomoserine sulfhydrylase MetY. The deletion of metY results in methionine auxotrophic strains grown on methanethiol or dimethyldisulfide as sole sulfur sources. In vitro studies with the wild-type reveal a relatively low activity of MetY for methanethiol and dimethyldisulfide
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
182000
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gel filtration, mutant strain No. 17, sucrose density gradient centrifugation, O-acetylhomoserine sulfhydrylase activity
194000
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sucrose density gradient centrifugation, wild-type, OAS-OAH sulfhydrylase with O-acetylserine as substrate
196000
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sucrose density gradient centrifugation, wild-type, OAS-OAH sulfhydrylase with O-acetylhomoserine as substrate
43000
480000
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gel filtration, larger than, no correct value could be estimated
57000
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4 * 57000, gel filtration in presence of urea and beta-mercaptoethanol
96000
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sucrose density gradient centrifugation , wild-type, O-acetylserine sulfhydrylase activity
99000
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gel filtration, sucrose density gradient centrifugation , mutant strain No. 17, O-acetylserine sulfhydrylase activity
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
monomer
tetramer
dimer
Corynebacterium acetophilum A51
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2 * 110000, SDS-PAGE
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tetramer
4 * 46000, SDS-PAGE, 4 * 46355, calculated from sequence
tetramer
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4 * 57000, gel filtration in presence of urea and beta-mercaptoethanol
tetramer
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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4 * 46059, calculated from amino acid sequence
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tetramer
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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4 * 46000, calculated from OAH1 sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.2 A resolution, space group C2, two monomers per asymmetric unit. The monomer adopts an alpha/beta fold and consists of a large central seven-stranded beta-sheet, a two-stranded beta-sheet and a three-stranded beta-sheet. The beta-sheets are flanked by a total of 12 alpha-helices and two 3(10)-helices. The active site is located near the N-terminus of alpha3. The pydridoxal 5'-phosphate-binding site is occupied by water molecules in the absence of the cofactor. The phosphate group of pydridoxal 5'-phosphate makes hydrogen bonds to Thr204, Ser202 and the amide N-atoms of Gly83 and Met84. Asp180 is within salt-bridge distance of the N1 atom of pydridoxal 5'-phosphate. Leu353, Met183, Ile87 and Met84 interact with the hydrophobic region of pydridoxal 5'-phosphate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 65
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activity decreases at about 40°C and is completely lost at 65°C
90
additional information
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no loss of activity after incubation at temperatures up to 60°C for 30 min at pH 7.5
90
Q93I77
very stable at high temperatures, 90% activity at 90°C for 60 min at pH 7.8
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme remains stable after purification, no dilution inactivation is observed
-
existence of glycerol in the purification buffer keeps the enzyme very stable, sensitive to salts such as (NH4)2SO4 and NaCl in absence of glycerol
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very unstable, can be stabilized by addition of 25% sucrose or glycerol
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 1 week, stable for at least 6 weeks if stabilized by addition of 20% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
oah1 gene cloned, sequenced and overexpressed in Escherichia coli BL21(DE3)
Q93I77
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
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overexpression of gene metY increases the in vitro activity of O-acetylhomoserine aminocarboxypropyltransferase to 1780 mU/mg and is beneficial for methionine production, since the intracellular methionine pool increases 2fold in the engineered strain
medicine
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no association of the polymorphisms A2756G in methionine synthase gene, C677T and A1298C in methylenetetrahydrofolate reductase gene, and 2R-3R in thymidylate synthase gene with increased risk for multiple myeloma
medicine
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no significant difference in polymorphism A2756G distribution is observed between controls and patients with esophageal squamous cell carcinoma. There is no association between methionine synthase A2756G polymorphism and the cystathionine beta-synthase 844ins68 insertion polymorphism and cancer of the upper gastrointestinal tract
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morinaga, Y.; Tani, Y.; Yamada, H.
Biosynthesis of homocysteine in a facultative methylotroph, Pseudomonas FM518
Agric. Biol. Chem.
47
2855-2860
1983
Pseudomonas sp., Pseudomonas sp. FM518
-
brenda
Yamagata, S.; Takeshima, K.; Naiki, N.
Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast
J. Biochem.
75
1221-1229
1974
Saccharomyces cerevisiae
brenda
Yamagata, S.; Takeshima, K.
O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme
J. Biochem.
80
777-785
1976
Saccharomyces cerevisiae
brenda
Yamagata, S.
O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure
J. Biochem.
80
787-797
1976
Saccharomyces cerevisiae
brenda
Yamagata, S.
Occurrence of low molecular weight O-acetylserine sulfhydrylase in the yeast Saccharomyces cerevisiae
J. Biochem.
88
1419-1423
1980
Saccharomyces cerevisiae
brenda
Smith, I.K.; Thompson, J.F.
Utilization of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies
Biochim. Biophys. Acta
184
130-138
1969
Neurospora sp.
brenda
Kerr, D.S.
O-Acetylhomoserine sulfhydrylase (Neurospora)
Methods Enzymol.
17
446-450
1971
Neurospora crassa
-
brenda
Kerr, D.S.
O-Acetylhomoserine sulfhydrylase from Neurospora. Purification and consideration of its function in homocysteine and methionine synthesis
J. Biol. Chem.
246
95-102
1971
Neurospora crassa
brenda
Yamagata, S.
Homocysteine in yeast. Partial purification and properties of O-acetylhomoserine sulfhydrylase
J. Biochem.
70
1035-1045
1971
Saccharomyces cerevisiae
brenda
Yamagata, S.; Takeshima, K.; Naiki, N.
O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast; studies with methionine auxotrophs
J. Biochem.
77
1029-1036
1975
Saccharomyces cerevisiae
brenda
Murooka,Y.; Kakihara, K.; Miwa, T.; Seto, K.; Harada, T.
O-Alkylhomoserine synthesis catalyzed by O-acetylhomoserine sulfhydrylase in microorganisms
J. Bacteriol.
130
62-73
1977
Corynebacterium acetophilum, Corynebacterium acetophilum A51
brenda
Ozaki, H.; Shiio, I.
Methionine biosynthesis in Brevibacterium flavum: Properties and essential role of O-acetylhomoserine sulfhydrylase
J. Biochem.
91
1163-1171
1982
[Brevibacterium] flavum
brenda
Yamagata, S.
O-Acetylhomoserine sulfhydrylase of the fission yeast Schizosaccharomyces pombe: Partial purification, characterization, and its probable role in homocysteine biosynthesis
J. Biochem.
96
1511-1523
1984
Schizosaccharomyces pombe
brenda
Chocat, P.; Esaki, N.; Tanaka, H.; Soda, K.
Synthesis of selenocystine and selenohomocystine with O-acetylhomoserine sulfhydrylase
Agric. Biol. Chem.
49
1143-1150
1985
Saccharomyces cerevisiae
-
brenda
Yamagata, S.; Paszewski, A.; Lewandowska, I.
Purification and properties of O-acetyl-L-homoserine O-sulfhydrylase from Aspergillus nidulans
J. Gen. Appl. Microbiol.
36
137-141
1990
Aspergillus nidulans, Aspergillus nidulans sG8
-
brenda
Brzywczy, J.; Yamagata, S.; Paszewski, A.
Comparative studies on O-acetylhomoserine sulfhydrylase: physiological role and characterization of the Aspergillus nidulans enzyme
Acta Biochim. Pol.
40
421-427
1993
Aspergillus nidulans, Aspergillus nidulans sG8
brenda
Yamagata, S.; Isaji, M.; Nakamura, K.; Fujisaki, S.; Doi, K.; Bawden, S.; D'Andrea, R.
Overexpression of the Saccharomyces cerevisiae MET17/MET25 gene in Escherichia coli and comparative characterization of the product with O-acetylserine-O-acetylhomoserine sulfhydrylase of the yeast
Appl. Microbiol. Biotechnol.
42
92-99
1994
Saccharomyces cerevisiae
brenda
Shimizu, H.; Yamagata, S.; Masui, R.; Inoue,Y.; Shibata, T.; Yokoyama, S.; Kuramitsu, S.; Iwama, T.
Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product
Biochim. Biophys. Acta
1549
61-72
2001
Thermus thermophilus (Q93I77), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q93I77)
brenda
Lambert, B.D.; Titgemeyer, E.C.; Stokka, G.L.; DeBey, B.M.; Loest, C.A.
Methionine supply to growing steers affects hepatic activities of methionine synthase and betaine-homocysteine methyltransferase, but not cystathionine synthase
J. Nutr.
132
2004-2009
2002
Bos taurus
brenda
Hacham, Y.; Gophna, U.; Amir, R.
In vivo analysis of various substrates utilized by cystathionine gamma-synthase and O-acetylhomoserine sulfhydrylase in methionine biosynthesis
Mol. Biol. Evol.
20
1513-1520
2003
Saccharomyces cerevisiae (P06106), Leptospira meyeri (P94890), Leptospira meyeri
brenda
Iwama, T.; Hosokawa, H.; Lin, W.; Shimizu, H.; Kawai, K.; Yamagata, S.
Comparative characterization of the oah2 gene homologous to the oah1 of Thermus thermophilus HB8
Biosci. Biotechnol. Biochem.
68
1357-1361
2004
Thermus thermophilus (Q76K51), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q76K51)
brenda
Qin, X.; Martin, S.A.
Cloning of the O-acetylhomoserine sulfhydrylase gene from the ruminal bacterium selenomonas ruminantium HD4
CURR. MICROBIOL.
48
305-311
2004
Selenomonas ruminantium (AY257545), Selenomonas ruminantium, Selenomonas ruminantium HD4 (AY257545), Selenomonas ruminantium HD4
brenda
Omura, H.; Ikemoto, M.; Kobayashi, M.; Shimizu, S.; Yoshida, T.; Nagasawa, T.
Purification, characterization and gene cloning of thermostable o-acetyl-L-homoserine sulfhydrylase forming gamma-cyano-alpha-aminobutyric acid
J. BIOSCI. BIOENG.
96
53-58
2003
Geobacillus stearothermophilus, Geobacillus stearothermophilus CN3
brenda
Yeom, H.J.; Hwang, B.J.; Lee, M.S.; Kim, Y.; Lee, H.S.
Regulation of enzymes involved in methionine biosynthesis in Corynebacterium glutamicum
J. Microbiol. Biotechnol.
14
373-378
2004
Corynebacterium glutamicum
-
brenda
Matityahu, I.; Kachan, L.; Bar Ilan, I.; Amir, R.
Transgenic tobacco plants overexpressing the Met25 gene of Saccharomyces cerevisiae exhibit enhanced levels of cysteine and glutathione and increased tolerance to oxidative stress
Amino Acids
30
185-194
2006
Saccharomyces cerevisiae
brenda
Tang, C.; Zhang, Z.; Xu, B.; Li, M.; Liu, J.; Cui, J.
Two newly synthesized 5-methyltetrahydrofolate-like compounds inhibit methionine synthase activity accompanied by cell cycle arrest in G1/S phase and apoptosis in vitro
Anticancer Drugs
19
697-704
2008
Homo sapiens
brenda
Ott, N.; Geddert, H.; Sarbia, M.
Polymorphisms in methionine synthase (A2756G) and cystathionine beta-synthase (844ins68) and susceptibility to carcinomas of the upper gastrointestinal tract
J. Cancer Res. Clin. Oncol.
134
405-410
2008
Homo sapiens
brenda
Lima, C.S.; Ortega, M.M.; Ozelo, M.C.; Araujo, R.C.; De Souza, C.A.; Lorand-Metze, I.; Annichino-Bizzacchi, J.M.; Costa, F.F.
Polymorphisms of methylenetetrahydrofolate reductase (MTHFR), methionine synthase (MTR), methionine synthase reductase (MTRR), and thymidylate synthase (TYMS) in multiple myeloma risk
Leuk. Res.
32
401-405
2008
Homo sapiens
brenda
Tran, T.H.; Krishnamoorthy, K.; Begley, T.P.; Ealick, S.E.
A novel mechanism of sulfur transfer catalyzed by O-acetylhomoserine sulfhydrylase in the methionine-biosynthetic pathway of Wolinella succinogenes
Acta Crystallogr. Sect. D
67
831-838
2011
Wolinella succinogenes (Q7M844), Wolinella succinogenes
brenda
Yin, J.; Garen, C.R.; Bateman, K.; Yu, M.; Lyon, E.Z.; Habel, J.; Kim, H.; Hung, L.W.; Kim, C.Y.; James, M.N.
Expression, purification and preliminary crystallographic analysis of O-acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
67
959-963
2011
Mycobacterium tuberculosis (L7N4M1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (L7N4M1)
brenda
Bolten, C.J.; Schroeder, H.; Dickschat, J.; Wittmann, C.
Towards methionine overproduction in Corynebacterium glutamicum - methanethiol and dimethyldisulfide as reduced sulfur sources
J. Microbiol. Biotechnol.
20
1196-1203
2010
Corynebacterium glutamicum
brenda
Kulikova, V.V.; Revtovich, S.V.; Bazhulina, N.P.; Anufrieva, N.V.; Kotlov, M.I.; Koval, V.S.; Morozova, E.A.; Hayashi, H.; Belyi, Y.F.; Demidkina, T.V.
Identification of O-acetylhomoserine sulfhydrylase, a putative enzyme responsible for methionine biosynthesis in Clostridioides difficile Gene cloning and biochemical characterizations
IUBMB Life
71
1815-1823
2019
Clostridioides difficile (Q187D4), Clostridioides difficile, Clostridioides difficile 630 (Q187D4)
brenda
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