Information on EC 2.5.1.6 - methionine adenosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.5.1.6
-
RECOMMENDED NAME
GeneOntology No.
methionine adenosyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
mechanism
-
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
steady state ordered Bi Ter mechanism with ATP adding before L-methionine and S-adenosylmethionine being the first product released, random release of phosphate and diphosphate
-
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
neutral H14 acts as an acid to cleave the C5-O5 bond of ATP, S of methionine makes a nucleophilic attack on the C5 to form the product
-
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
mechanism of inhibiton by product analogues and implications for reaction
-
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
mechanism, key role of K182 in the correct positioning of the substrates, and D135 in stabilizing the sulfonium group formed in the product
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
catalysis of a SN2 reaction through hydrogen bonding of the liberated oxygen-5' to the histidine, charge neutralization by the two Mg2+ ions, and stabilization of the product sulfonium cation through a close, non-bonded, contact between the sulfur and the ribose oxygen-4'
-
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
adenosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2'-deoxymugineic acid phytosiderophore biosynthesis
-
-
ethylene biosynthesis I (plants)
-
-
L-methionine degradation I (to L-homocysteine)
-
-
S-adenosyl-L-methionine biosynthesis
-
-
S-adenosyl-L-methionine cycle II
-
-
methionine metabolism
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-methionine S-adenosyltransferase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
adenosylmethionine synthetase
-
-
-
-
AdoMet synthease
-
-
AdoMet synthease
Crypthecodinium cohnii (Biecheler)
-
-
-
AdoMet synthetase
-
-
-
-
AdoMet synthetase
-
AdoMet synthetase
-
AdoMet synthetase
-
AdoMet synthetase
-
AdoMetS
Crypthecodinium cohnii (Biecheler)
-
-
-
ATP-methionine adenosyltransferase
-
-
-
-
ATP: L-methionine S-adenosyltransferase
-
-
EC 2.4.2.13
-
-
formerly
-
MAT
-
-
MAT III
-
isozyme
MAT2
Leishmania infantum LEM75
-
-
-
MAT2A
-
-
MAT2A
-
part of the catalytic subunit
MAT2beta
-
regulatory subunit
methionine adenosyl transferase 2A
-
-
methionine adenosyltransferase
-
-
-
-
methionine adenosyltransferase
-
-
methionine adenosyltransferase 2A
-
-
methionine adenosyltransferase 2A
-
methionine adenosyltransferase 2beta
-
-
methionine adenosyltransferase II
-
methionine S-adenosyltransferase
-
-
-
-
methionine-activating enzyme
-
-
-
-
PF1866
gene name
S-adenosyl-L-methionine synthetase
-
-
-
-
S-adenosyl-L-methionine synthetase
-
S-adenosyl-Lmethionine synthetase
-
-
S-adenosyl-Lmethionine synthetase
Leishmania infantum LEM75
-
-
-
S-adenosylmethionine synthase
-
-
-
-
S-adenosylmethionine synthase
-
-
S-adenosylmethionine synthetase
-
-
-
-
S-adenosylmethionine synthetase
-
-
S-adenosylmethionine synthetase
-
S-adenosylmethionine synthetase
-
-
S-adenosylmethionine synthetase
Crypthecodinium cohnii (Biecheler)
-
-
-
S-adenosylmethionine synthetase
-
S-adenosylmethionine synthetase
-
S-adenosylmethionine synthetase
-
S-adenosylmethionine synthetase
-
S-adenosylmethionine synthetase
-
-
S-adenosylmethionine synthetase
-
-
S-adenosylmethionine synthetase
-
-
S-adenosylmethionine synthetase 2
-
S-adenosylmethionine synthetase A
-
-
S-adenosylmethionine synthetase B
-
-
S-adenosylmethionine-L-synthetase
-
SAM synthetase
-
-
SAM synthetase
-
SAM synthetase
-
-
SAMS2
-
-
SSO0199
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
9012-52-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozymes MAT1, MAT2, and MAT3
-
-
Manually annotated by BRENDA team
isozyme SAMS1; a halophyte, isozyme SAMS1
SwissProt
Manually annotated by BRENDA team
isozyme SAMS2; a halophyte, isozyme SAMS2
SwissProt
Manually annotated by BRENDA team
isozyme SAMS3; a halophyte, isozyme SAMS3
SwissProt
Manually annotated by BRENDA team
isozyme SAMS4; a halophyte, isozyme SAMS4
SwissProt
Manually annotated by BRENDA team
gene metK, strain ZB307Spc
-
-
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
SAMS1; Madagascar perwinkle, L. G. Don, line CP3a, three isoenzymes: SAMS 1, 2 and 3
SwissProt
Manually annotated by BRENDA team
SAMS2; Madagascar perwinkle, L. G. Don, line CP3a, three isoenzymes: SAMS 1, 2 and 3
SwissProt
Manually annotated by BRENDA team
SAMS3; Madagascar perwinkle, L. G. Don, line CP3a, three isoenzymes: SAMS 1, 2 and 3
SwissProt
Manually annotated by BRENDA team
strain (Biecheler) 1649
-
-
Manually annotated by BRENDA team
Crypthecodinium cohnii (Biecheler)
strain (Biecheler) 1649
-
-
Manually annotated by BRENDA team
a pathogenic piscine hemoflagellate, gene metK or MAT
SwissProt
Manually annotated by BRENDA team
gene metK, strain BW25113
-
-
Manually annotated by BRENDA team
XL1-Blue strain
Uniprot
Manually annotated by BRENDA team
Escherichia coli XL1-Blue
XL1-Blue strain
Uniprot
Manually annotated by BRENDA team
3 isoenzymes: MAT-I, MAT-II, MAT-III
-
-
Manually annotated by BRENDA team
genes MAT1A and MAT2A, isozymes MAT I-MAT III
-
-
Manually annotated by BRENDA team
isoforms MAT1A, MAT2A
-
-
Manually annotated by BRENDA team
lung epithelial isoform and Jurkat cell isozyme of MAT 2A
UniProt
Manually annotated by BRENDA team
MAT-II
SwissProt
Manually annotated by BRENDA team
strain GS115
-
-
Manually annotated by BRENDA team
strain LEM75
-
-
Manually annotated by BRENDA team
Leishmania infantum LEM75
strain LEM75
-
-
Manually annotated by BRENDA team
hypertermophilic archaeon
-
-
Manually annotated by BRENDA team
isozymes MAT I-MAT III
-
-
Manually annotated by BRENDA team
mouse, 2 isoenzymes: I and II
-
-
Manually annotated by BRENDA team
2 forms: high-MW form and low-MW form
-
-
Manually annotated by BRENDA team
3 isoenzymes: MAT-I, MAT-II, MAT-III
-
-
Manually annotated by BRENDA team
isoforms MAT1A, MAT2A
-
-
Manually annotated by BRENDA team
recombinant enzyme, isoform MAT I, tetramer, and MAT III, dimer
UniProt
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
tetrameric form MAT I
UniProt
Manually annotated by BRENDA team
two MAT III isoforms
-
-
Manually annotated by BRENDA team
gene metK, fever group, Breinl and Madrid E strains
-
-
Manually annotated by BRENDA team
gene metK, strain Wilmington of the typhus group rickettsiae
-
-
Manually annotated by BRENDA team
2 forms: I and II
-
-
Manually annotated by BRENDA team
induction by salinity stress
-
-
Manually annotated by BRENDA team
strain NRRL8165, gene SAM-s
Uniprot
Manually annotated by BRENDA team
KO-179 strain. Actinorhodin-overproducer
Uniprot
Manually annotated by BRENDA team
KO-179 strain. Actinorhodin-overproducer
Uniprot
Manually annotated by BRENDA team
isoform MetK1; strain ATCC 27952
UniProt
Manually annotated by BRENDA team
isoform MetK2; strain ATCC 27952
UniProt
Manually annotated by BRENDA team
; 2 forms: A and B
-
-
Manually annotated by BRENDA team
7 to 8-d-old piglets, milk from lactating sows
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
subunit MAT2beta
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme plays a key role in the biogenesis of S-adenosyl-L-methionine
physiological function
-
MAT2A or MAT2beta silencing results in decreased collagen and alpha-smooth muscle actin expression and cell growth and increased apoptosis. MAT2A knockdown decreases intracellular S-adenosylmethionine levels in LX-2 cells. Activation of extracellular signal-regulated kinase and phosphatidylinositol-3-kinase signaling in LX-2 cells requires the expression of MAT2 but not that of MAT2A
physiological function
-
MAT2A silencing in primary heaptic stellate cells results in decreased collagen and alpha-smooth muscle actin expression and cell growth and increased apoptosis
physiological function
doxorubicin production by the metK1-sp-deleted mutant is reduced
physiological function
-
the enzyme is involved in biosynthesis of S-adenosyl-L-methionine
physiological function
-
the enzyme is involved in biosynthesis of S-adenosyl-L-methionine
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
ir
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
completely specific for ATP
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
ir
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
completely specific for ATP
-
-
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylselanyl)butanoic acid
show the reaction diagram
10% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(but-3-yn-1-ylsulfanyl)butanoic acid
show the reaction diagram
30% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(butylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(butylselanyl)butanoic acid
show the reaction diagram
70% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(butylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(butylsulfanyl)butanoic acid
show the reaction diagram
27% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(ethylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(ethylselanyl)butanoic acid
show the reaction diagram
76% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(ethylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(ethylsulfanyl)butanoic acid
show the reaction diagram
84% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(prop-2-en-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(prop-2-en-1-ylselanyl)butanoic acid
show the reaction diagram
30% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(prop-2-en-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(prop-2-en-1-ylsulfanyl)butanoic acid
show the reaction diagram
27% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(prop-2-yn-1-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(prop-2-yn-1-ylselanyl)butanoic acid
show the reaction diagram
28% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(prop-2-yn-1-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(prop-2-yn-1-ylsulfanyl)butanoic acid
show the reaction diagram
36% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(propan-2-ylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(propan-2-ylselanyl)butanoic acid
show the reaction diagram
40% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(propan-2-ylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(propan-2-ylsulfanyl)butanoic acid
show the reaction diagram
53% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(propylselanyl)butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-(propylselanyl)butanoic acid
show the reaction diagram
66% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-(propylsulfanyl)butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-(propylsulfanyl)butanoic acid
show the reaction diagram
44% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(2-azido ethyl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2-azido ethyl)sulfanyl]butanoic acid
show the reaction diagram
50% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(2-methyl propyl)sulfanyl] butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2-methyl propyl)sulfanyl]butanoic acid
show the reaction diagram
57% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(2-methylprop-2-en-1-yl)selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[(2-methylprop-2-en-1-yl)selanyl]butanoic acid
show the reaction diagram
46% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(2-methylprop-2-en-1-yl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2-methylprop-2-en-1-yl)sulfanyl]butanoic acid
show the reaction diagram
15% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(2E)-but-2-en-1-ylsulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2E)-but-2-en-1-ylsulfanyl]butanoic acid
show the reaction diagram
27% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(2E)-penta-2,4-dien-1-ylsulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(2E)-penta-2,4-dien-1-ylsulfanyl]butanoic acid
show the reaction diagram
25% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(3-azido propyl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(3-azido propyl)sulfanyl]butanoic acid
show the reaction diagram
60% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(3-methyl butyl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(3-methyl butyl)sulfanyl] butanoic acid
show the reaction diagram
36% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(3-methylbut-2-en-1-yl)selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[(3-methylbut-2-en-1-yl)selanyl]butanoic acid
show the reaction diagram
44% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(3-methylbut-2-en-1-yl)sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(3-methylbut-2-en-1-yl)sulfanyl]butanoic acid
show the reaction diagram
12% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(cyanomethyl) sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(cyanomethyl) sulfanyl]butanoic acid
show the reaction diagram
68% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[(cyanomethyl)selanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[(cyanomethyl) selanyl]butanoic acid
show the reaction diagram
12% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[[(2E)-4-aminobut-2-en-1-yl]selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[[(2E)-4-aminobut-2-en-1-yl]selanyl]butanoic acid
show the reaction diagram
38% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]selanyl]butanoic acid + H2O
phosphate + diphosphate + Se-adenosyl-(2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]selanyl]butanoic acid
show the reaction diagram
24% of the turnover rate compared to L-methionine
-
?
ATP + (2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]sulfanyl]butanoic acid + H2O
phosphate + diphosphate + S-adenosyl-(2S)-2-amino-4-[[(2E)-4-azidobut-2-en-1-yl]sulfanyl]butanoic acid
show the reaction diagram
28% of the turnover rate compared to L-methionine
-
?
ATP + D-methionine + H2O
S-adenosyl-D-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
show the reaction diagram
-
-
-
-
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
show the reaction diagram
-
-
-
-
ATP + L-ethionine + H2O
phosphate + diphosphate + S-adenosyl-L-ethionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
ir
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
mechanism
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
completely specific for ATP
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
the product S-adenosylmethionine is important as a direct metabolic donor of methyl and alpha-amino-n-butyryl groups
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
used as aminopropyl group donor in synthesis of polyamines and is also the methyl group donor for most cellular methyltransferase reactions
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
methyl donor in transmethylation reactions and as propylamine donor for polyamine biosynthesis
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
two reaction steps: S-adenosylmethionine synthesis and tripolyphosphate hydrolysis. Tripolyphosphate hydrolysis is the rate determining reaction
-
-
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
MAT activity controls cellular glutathione levels, polyamine synthesis and folate cycling
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
a post-translational mechanism is involved in MAT regulation, the enzyme is down-regulated in pathological processes such as liver cirrhosis, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
an essential enzyme that catalyzes the formation of the principal methyl donor S-adenosylmethionine, S-adenosyl-L-methionine is also a key metabolite that regulates hepatocyte growth, death and differentiation, molecular mechanism, overview, abnormalities in MAT and decreased S-adenosyl-L-methionine levels occur in humans with alcoholic liver disease, chronic hepatic S-adenosyl-L-methionine deficiency can result in the spontaneous development of steatohepatitis and hepatocellular carcinoma, overview, hepatic S-adenosyl-L-methionine biosynthesis and methionine metabolism, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
aspartate family biosynthesis pathway and methionine metabolism, regulation, S-adenosyl-L-methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
aspartate family biosynthesis pathway and methionine metabolism,regulation, S-adenosyl-L.methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
biosynthesis of the key compound in the trans-methylation reactions
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
rate-limiting enzyme of the S-adenosyl-L-methionine synthesis pathway, cell methionine and S-adenosylmethionine contents increase in response to hyperoxia in SAE and A549 cells, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
regulation of methionine metabolism, S-adenosyl-L-methionine metabolic pathway, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
S-adenosyl-L-methionine is required for betaine synthesis and also for the synthesis of other compounds, especially lignin, transcript levels of the enzyme are co-regulated with those of phosphoethanolamine N-methyltransferase and choline monooxygenase to supply S-adenosyl-L-methionine for betaine synthesis in the leaves, overview, enzyme regulation pattern in plant tissues, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
the S(MK) box, a conserved RNA motif in the 5'-untranslated region of the metK gene, is a SAM-binding RNA responsible for translational regulation of the enzyme, it binds specifically to S-adenosyl-L-methionine in vitro and in vivo causing a structural RNA rearrangement that causes a sequestration of the Shine-Dalgarno sequence, structural mapping and mechanism, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
typhus group rickettsiae have the capability of synthesizing as well as transporting SAM
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
biosynthesis of S-adenosyl-L-methionine, two-step reaction in which reaction of ATP and methionine initially yields the S-adenosyl-L-methionine and tripolyphosphate. The tripolyphosphate remains enzyme-bound and is cleaved to diphosphate and phosphate before product release
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
the enzyme plays a key role in the biogenesis of S-adenosyl-L-methionine
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
Crypthecodinium cohnii (Biecheler)
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
biosynthesis of S-adenosyl-L-methionine, two-step reaction in which reaction of ATP and methionine initially yields the S-adenosyl-L-methionine and tripolyphosphate. The tripolyphosphate remains enzyme-bound and is cleaved to diphosphate and phosphate before product release
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
Leishmania infantum LEM75
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
?
ATP + L-methionine methyl ester + H2O
S-adenosyl-L-methionine methyl ester + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-selenomethionine + H2O
phosphate + diphosphate + Se-adenosyl-L-selenomethionine
show the reaction diagram
as active as L-methionine
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
CTP + L-methionine + H2O
S-cytosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
GTP + L-methionine + H2O
S-guanosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
two isoenzymes with different behavior on exogenous S-adenosylmethionine addition
-
?
UTP + L-methionine + H2O
S-urasyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
ATP can be substituted by 3'-deoxy-ATP,8-bromo-ATP, formycin triphosphate, adenyl-5'yl imidodiphosphate
-
-
-
additional information
?
-
-
ATP can be substituted by 3'-deoxy-ATP,8-bromo-ATP, formycin triphosphate, adenyl-5'yl imidodiphosphate, methionine can be substituted by selenomethionine, alpha-methyl-DL-methionine
-
-
-
additional information
?
-
-
no activity with methional, methioninol, 3-methylthiopropylamine
-
-
-
additional information
?
-
S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants
-
-
-
additional information
?
-
-
genes in the S-box family are regulated by binding of S-adenosylmethionine to the 5' region of the mRNA of the regulated gene, SAM binding promotes a rearrangement of the RNA structure that results in premature termination of transcription in vitro and repression of expression of the downstream coding sequence, the S-box RNA element therefore acts as a SAM-binding riboswitch in vitro
-
-
-
additional information
?
-
-
protein S-nitrosylation by NO represents a redox-based regulation mechanism playing a pivotal role in plants, MAT catalyzes the synthesis of the ethylene precursor S-adenosylmethionine and NO influences ethylene production in plants, the enzyme probably mediates the cross-talk between ethylene and NO signaling, overview
-
-
-
additional information
?
-
transmethylation and transsulfuration pathways, overview
-
-
-
additional information
?
-
-
S-adenosylmethionine synthetase A exhibits tripolyphosphatase activity, S-adenosylmethionine synthetase B exhibits tripolyphosphatase activity
-
-
-
additional information
?
-
the enzyme has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
ir
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
the product S-adenosylmethionine is important as a direct metabolic donor of methyl and alpha-amino-n-butyryl groups
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
used as aminopropyl group donor in synthesis of polyamines and is also the methyl group donor for most cellular methyltransferase reactions
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
methyl donor in transmethylation reactions and as propylamine donor for polyamine biosynthesis
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
two reaction steps: S-adenosylmethionine synthesis and tripolyphosphate hydrolysis. Tripolyphosphate hydrolysis is the rate determining reaction
-
-
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
MAT activity controls cellular glutathione levels, polyamine synthesis and folate cycling
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
Q3HW35
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
a post-translational mechanism is involved in MAT regulation, the enzyme is down-regulated in pathological processes such as liver cirrhosis, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
an essential enzyme that catalyzes the formation of the principal methyl donor S-adenosylmethionine, S-adenosyl-L-methionine is also a key metabolite that regulates hepatocyte growth, death and differentiation, molecular mechanism, overview, abnormalities in MAT and decreased S-adenosyl-L-methionine levels occur in humans with alcoholic liver disease, chronic hepatic S-adenosyl-L-methionine deficiency can result in the spontaneous development of steatohepatitis and hepatocellular carcinoma, overview, hepatic S-adenosyl-L-methionine biosynthesis and methionine metabolism, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
aspartate family biosynthesis pathway and methionine metabolism, regulation, S-adenosyl-L-methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
aspartate family biosynthesis pathway and methionine metabolism,regulation, S-adenosyl-L.methionine activates threonine synthase expression and negatively regulates the transcript level of the cystathionine gamma-synthase, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
Q6J2L0
biosynthesis of the key compound in the trans-methylation reactions
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
P31153
rate-limiting enzyme of the S-adenosyl-L-methionine synthesis pathway, cell methionine and S-adenosylmethionine contents increase in response to hyperoxia in SAE and A549 cells, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
regulation of methionine metabolism, S-adenosyl-L-methionine metabolic pathway, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
Q6F3F0, Q6F3F1, Q6F3F3, Q7XZR1
S-adenosyl-L-methionine is required for betaine synthesis and also for the synthesis of other compounds, especially lignin, transcript levels of the enzyme are co-regulated with those of phosphoethanolamine N-methyltransferase and choline monooxygenase to supply S-adenosyl-L-methionine for betaine synthesis in the leaves, overview, enzyme regulation pattern in plant tissues, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
the S(MK) box, a conserved RNA motif in the 5'-untranslated region of the metK gene, is a SAM-binding RNA responsible for translational regulation of the enzyme, it binds specifically to S-adenosyl-L-methionine in vitro and in vivo causing a structural RNA rearrangement that causes a sequestration of the Shine-Dalgarno sequence, structural mapping and mechanism, overview
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
typhus group rickettsiae have the capability of synthesizing as well as transporting SAM
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
biosynthesis of S-adenosyl-L-methionine
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
Q8TZW1
the enzyme plays a key role in the biogenesis of S-adenosyl-L-methionine
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
biosynthesis of S-adenosyl-L-methionine
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
?
additional information
?
-
-
genes in the S-box family are regulated by binding of S-adenosylmethionine to the 5' region of the mRNA of the regulated gene, SAM binding promotes a rearrangement of the RNA structure that results in premature termination of transcription in vitro and repression of expression of the downstream coding sequence, the S-box RNA element therefore acts as a SAM-binding riboswitch in vitro
-
-
-
additional information
?
-
-
protein S-nitrosylation by NO represents a redox-based regulation mechanism playing a pivotal role in plants, MAT catalyzes the synthesis of the ethylene precursor S-adenosylmethionine and NO influences ethylene production in plants, the enzyme probably mediates the cross-talk between ethylene and NO signaling, overview
-
-
-
additional information
?
-
P31153
transmethylation and transsulfuration pathways, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
0.02 mM stimulates activity
Co2+
-
for maximal activation the cation concentration must be at least equal to ATP concentration
Co2+
-
can replace Mg2+ with a lower relative activity, S-adenosylmethionine synthetase B; can replace Mg2+ with lower relative activity
Co2+
0.02 mM stimulates activity
K+
-
activation at 25-50 mM
K+
-
both Mg2+ and K+ required for full activity
K+
-
absolute requirement, cannot be replaced by Na+
K+
monovalent cations required for optimal activity, 50 mM K+ sufficient for full activity, can be replaced by NH4+ but not by Na+; monovalent cations required for optimal activity, 50 mM K+ sufficient for full activity, can be replaced by NH4+ but not by Na+; monovalent cations required for optimal activity, 50 mM K+ sufficient for full activity, can be replaced by NH4+ but not by Na+
K+
-
enhances Kcat and decrees Km values for both substrates
K+
0.2 mM stimulates activity
K+
-
slight activation
K+
-
half-maximal activation at 25 mM KCl
Mg2+
-
optimal concentration at 10-20 mM
Mg2+
-
both Mg2+ and K+ required for full activity
Mg2+
-
absolute requirement
Mg2+
-
maximal activation at 40 mM; S-adenosylmethionine synthetase A is absolutely dependent upon the presence of Mg2+, suggesting that a Mg-ATP complex functions as substrate. Maximal activity is obtained at an Mg2+ concentration of 40 mM with 10 mM ATP. 30% of the maximal reaction rate is observable at equimolar concentrations of ATP and Mg2+ (10 mM); S-adenosylmethionine synthetase B is absolutely dependent upon the presence of Mg2+, suggesting that a Mg-ATP complex functions as substrate. Maximal activity is obtained at an Mg2+ concentration of 40 mM with 10 mM ATP. 30% of the maximal reaction rate is observable at equimolar concentrations of ATP and Mg2+ (10 mM)
Mg2+
-
Mg2+ in excess of that bound to ATP and EDTA is required for optimal activity
Mg2+
-
absolute requirement, cannot be replaced by Mn2+
Mg2+
-
cation concentration must be at least equal to ATP concentration for maximal activity
Mg2+
-
-
Mg2+
strictly dependent on divalent cations with maximum activity at 5mM and Mg2+ fully replaceable by Mn2+ or Co2+ salts; strictly dependent on divalent cations with maximum activity at 5mM and Mg2+ fully replaceable by Mn2+ or Co2+ salts; strictly dependent on divalent cations with maximum activity at 5mM and Mg2+ fully replaceable by Mn2+ or Co2+ salts
Mg2+
-
cannot be replaced by Ca2+
Mg2+
-
absolute requirement
Mg2+
the enzyme requires Mn2+ or Mg2+, which are equally active, bound by D17 and D289
Mg2+
-
-
Mg2+
required for activity
Mg2+
-
up to 20% activation
Mg2+
-
no activity is detectable in the absence of Mg2+, and maximal activity is observed at 10 mM MgCl2 when ATP is present at 5 mM, indicating that MgATP is probably the true substrate
Mg2+
absolutely dependent upon the presence of Mg2+, suggesting that a Mg2+-ATP complex functions as substrate. Maximal activity is obtained at a Mg2+ concentration of 20 mM
Mn2+
-
optimal concentration at 2 mM
Mn2+
-
for maximal activation the cation concentration must be at least equal to ATP concentration
Mn2+
-
can partially replace Mg2+ in activation, inhibition in presence of Mg2+
Mn2+
-
can replace Mg2+ with a lower relative activity, S-adenosylmethionine synthetase A; can replace Mg2+ with a lower relative activity, S-adenosylmethionine synthetase B; can replace Mg2+ with lower relative activity
Mn2+
the enzyme requires Mn2+ or Mg2+, which are equally active
Na+
-
slight activation in absence of Mg2+
NH4+
-
activity is dependent on both divalent Mg2+ or Mn2+ and monovalent cations NH4+ or K+
Ni2+
0.02 mM stimulates activity
Zn2+
66% of the activity with Mg2+ or Mn2+
Zn2+
0.02 mM stimulates activity
Mn2+
-
slight activiation
additional information
-
divalent cations are required for tripolyphosphatase activity
additional information
Ag+, Ca2+, Fe2+, and Cu2+ cannot substitue for Mg2+ or Mn2+
additional information
-
Mg2+, H2PO4-, NH4-, and NO3- have no significant effect on enzyme activity at 5 mM
additional information
no stimulatory effect by K+ has been observed even at high concentration (40 mM)
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,4S)-amino-4,5-epoxypentanoic acid
-
1-(3-(2-ethoxyphenyl)ureidoacetyl)-4-(2-methyl-5-nitrophenyl)semicarbazide
-
binding to adenosyl region of the active site
1-(4-chloro-2-nitrophenyl)-3-(4-sulfamoylphenyl)-urea
-
binding to adenosyl region of the active site
1-aminocyclopentanecarboxylic acid
-
-
1-methyluric acid
10 mM, 43.4% inhibition
1-Methylxanthine
10 mM, 35.9% inhibition
2,6-Diaminopurine
10 mM, 29.3% inhibition
2,6-dichloropurine
10 mM, 35.5% inhibition
2-amino-6-carboxyethylmercaptopurine
10 mM, 31.9% inhibition
2-amino-6-chloropurine riboside
10 mM, 17.2% inhibition
2-amino-6-chloropurine-9-acetic acid
10 mM, 23.5% inhibition
2-Aminopurine
10 mM, 11.0% inhibition
2-Hydroxypurine
10 mM, 33.8% inhibition
3,7-dimethyluric acid
10 mM, 27.9% inhibition
3-morpholinosydnoniimide
-
loss of liver MAT activity in vivo
5-amino-L-norvaline
10-25% inhibition with 5 mM; 10-25% inhibition with 5 mM; 10-25% inhibition with 5 mM
5-azacytidine
-
0.2 mM leads to significant reduction of AdoMetS protein expression
6-benzyloxypurine
10 mM, 17.7% inhibition
6-bromopurine
10 mM, 31.4% inhibition
6-Chloropurine
10 mM, 31.4% inhibition
6-Chloropurine riboside
10 mM, 17.1% inhibition
6-Cyanopurine
10 mM, 24.2% inhibition
6-dimethylallylaminopurine riboside
10 mM, 41.6% inhibition
6-Dimethylaminopurine
10 mM, 28.0% inhibition
6-Mercaptopurine
10 mM, 40.1% inhibition
6-mercaptopurine riboside
10 mM, 30.0% inhibition
6-propoxypurine
10 mM, 27.9% inhibition
7-hydroxypropyl theophylline
10 mM, 16.1% inhibition
7-Methyluric acid
10 mM, 11.4% inhibition
7-methylxanthine
10 mM, 36.3% inhibition
8-aza-2,6-diaminopurine
10 mM, 40.0% inhibition
8-Azaguanine
; 10 mM, 81.7% inhibition
8-chlorotheophylline
10 mM, 7.0% inhibition
Adenyl-5'-ylimidodiphosphate
-
competitive with ATP
ADP
35-50% inhibition with 5 mM; 35-50% inhibition with 5 mM; 35-50% inhibition with 5 mM
alpha,beta-methylene-adenosine tetraphosphate
-
-
alpha,beta-methylene-ATP
-
-
alpha-methyl-DL-methionine
10 mM, 18.8% inhibition
AMP
-
causes complete inactivation of the enzyme
ATP
-
ATP and methionine act as a switch between two different MAT III isoforms
ATP
-
causes complete inactivation of the enzyme
Azathioprine
; 10 mM, 75.5% inhibition
Ba2+
-
70.70% residual activity at 5 mM
bacterial lipopolysaccharide
-
decreases MAT activity in vivo
-
bacterial lipopolysaccharide
-
results in the accumulation of nitrites and nitrates in serum and in the inactivation of MAT I/III
-
beta,gamma-methylene-ATP
-
-
Br-
-
93.33% residual activity at 5 mM
Ca2+
-
86.36% residual activity at 5 mM
carbon tetrachloride
-
depletion of glutathione levels reduces MAT I/III activities in vivo
CH3COO-
-
92.25% residual activity at 5 mM
Cl-
-
85.27% residual activity at 5 mM
CTP
-
; 20 mM, 37% inhibition, S-adenosylmethionine synthetase B; 20 mM, 40% inhibition, S-adenosylmethionine synthetase A
CTP
60-70% inhibition with 5 mM; 60-70% inhibition with 5 mM; 60-70% inhibition with 5 mM
Cu2+
-
25.74% residual activity at 5 mM
Cu2+
isozyme subunit MATalpha2 is inhibited by 0.25 mM Cu2+ in the presence or absence of dithiothreitol, strong reduction in MAT2B gene expression induced by Cu2+ (60%), copper effects can only be prevented by buthionine sulfoximine, whereas N-acetylcysteine and neocuproine are ineffective
cycloleucine
-
25 mM, 56% inhibition, S-adenosylmethionine synthetase A; inhibits only at sub saturating concentrations of methionine
cycloleucine
10 mM, 25.8% inhibition
cycloleucine
-
competitive
cycloleucine
1-aminocyclopentane-1-carboxylic acid, specific MAT inhibitor
diimidotriphosphate
-
mechanism
Dimethylsulfoxide
-
weak inhibition of liver isoenzyme
Dimethylsulfoxide
-
-
Dimethylsulfoxide
-
-
Dimethylsulfoxide
-
slight inhibition of gamma isoenzyme from kidney
Dimethylsulfoxide
-
-
diphosphate
-
individually a weak inhibitor, in combination with phosphate there is a marked synergistic effect
diphosphate
-
; 20 mM, 30% inhibition, S-adenosylmethionine synthetase A; 20 mM, 49% inhibition, S-adenosylmethionine synthetase B
diphosphate
-
-
diphosphate
-
inhibits high-MW isoenzyme, no effect on low-MW enzyme
diphosphate
-
-
diphosphate
-
inhibition for S-adenosylmethionine and L-methonine
DL-2-Amino-trans-4-hexenoic acid
-
-
ethanol
25 mM ethanol substantially decreases the enzymatic activity of MAT II
Ethionine
32-38% inhibition with 5 mM; 32-38% inhibition with 5 mM; 32-38% inhibition with 5 mM
F-
-
88.84% residual activity at 5 mM
Fe2+
-
59.22% residual activity at 5 mM
Fumarylacetoacetate
-
reduces MAT I/III activity
glycerol
-
inhibits kidney isoenzyme gamma
GSH
-
causes complete inactivation of the enzyme
GTP
-
; 20 mM, 50% inhibition, S-adenosylmethionine synthetase B; 20 mM, 56% inhibition, S-adenosylmethionine synthetase A
GTP
not accepted as a substrate but inhibits the reaction in the presence of ATP, 70-80% inhibition with 5 mM; not accepted as a substrate but inhibits the reaction in the presence of ATP, 70-80% inhibition with 5 mM; not accepted as a substrate but inhibits the reaction in the presence of ATP, 70-80% inhibition with 5 mM
GTP
-
competitive with respect to ATP and noncompetitive with L-methionine
hydrogen peroxide
-
inactives CHO cells-MAT, prevented by desferoxamine. Time- and dose-dependent inactivation of MAT I/III, activity recovered by addition of glutathione
hydrogen peroxide
-
reduces MAT I/III activity
hydrogen peroxide
-
-
I-
-
87.91% residual activity at 5 mM
K+
-
above 50 mM
K+
-
85.27% residual activity at 5 mM
L-2-Amino-4-hexynoic acid
-
-
L-2-Amino-4-methoxy-cis-but-3-enoic acid
-
-
L-2-Amino-4-methoxy-cis-but-3-enoic acid
-
-
L-2-Amino-4-methylthio-cis-but-3-enoic acid
-
-
L-buthionine-(S,R)-sulfoximine
-
inhibits glutathione synthesis and this decreases MAT activity in vivo. Prevented by the administration of glutathione-ethyl ester
L-buthionine-(S,R)-sulfoximine
-
inactivates hepatic MAT, prevented by the administration of glutathione-ethyl ester
L-ethioninamide
10 mM, 23.9% inhibition
L-ethionine
-
competitive with respect to methionine for S-adenosylmethionine formation and noncompetitive with respect to ATP
L-ethionine
10 mM, 20.4% inhibition
L-ethionine
-
1.2 mM leads to significant reduction of AdoMetS protein expression
L-methionine
-
-
L-methionine
-
ATP and methionine act as a switch between two different MAT III isoforms
L-methionine
30% reduction in total activity is detected at 5 mM L-methionine; 30% reduction in total activity is detected at 5 mM L-methionine; 30% reduction in total activity is detected at 5 mM L-methionine
L-methionine methyl ester
10 mM, 17.7% inhibition
L-Methionine sulfone
10 mM, 9.2% inhibition
L-methionine sulfoxide
10 mM, 4.0% inhibition
L-methionine sulfoximine
10 mM, 12.6% inhibition
L-Penicillamine
10 mM, 15.0% inhibition
Li+
-
81.40% residual activity at 5 mM
methanol
2.4% methanol depresses methionine adenosyltransferase specific activity, this effect is not observed with 0.8% methanol
methylthio propionaldehyde
10 mM, 18.4% inhibition
methylthioadenosine
1 mM downregulates MAT2A expression
methylthioadenosine
-
lowers expression of MAT2A and MAT2beta
Mg2+
-
inhibitory above 8.5 mM
Mn2+
-
inhibition in presence of Mg2+
N-ethylmaleimide
-
time-dependent inactivation of both MAT activities
Na+
-
in presence of Mg2+
Na+
-
80.16% residual activity at 5 mM
nitric oxide
-
two MAT III isoforms, one with low tripolyphosphatase activity that is insensitive to NO and another with high tripolyphosphatase activity that is inhibited by NO
nitric oxide
-
inactivates hepatic MAT
nitrosoglutathione
-
reversibly inhibits the isozyme MAT1 via NO binding to Cys114, no inhibition of isozymes MAT2 and MAT3, molecular mechanism for S-nitrosylation of the enzyme
O-methylguanine
10 mM, 60.3% inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
alpha and beta isoenzymes completely inhibited, gamma isoenzyme slightly inhibited
p-chloromercuribenzoate
-
reduces MAT I/III activity
phosphate
-
individually a weak inhibitor, in combination with diphosphate there is a synergistic inhibitory effect
phosphate
-
; 10 mM, 19% inhibition, S-adenosylmethionine synthetase B; 10 mM, 45% inhibition, S-adenosylmethionine synthetase A
phosphate
-
-
phosphate
-
competitive toward both ATP and methionine
putrescine
15-25% inhibition with 5 mM; 15-25% inhibition with 5 mM; 15-25% inhibition with 5 mM
S-adenosyl-L-ethionine
-
-
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
not inhibitory
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-methionine
-
feedback inhibition of isozyme MAT II
S-adenosylmethionine
-
-
S-adenosylmethionine
-
inhibition of rat kidney enzyme and rat liver MAT-II, weak inhibition of rat liver MAT-I
S-adenosylmethionine
-
-
S-adenosylmethionine
-
inhibits the A form but not the B form; non-competitive, S-adenosylmethionine synthetase A; slight inhibition of S-adenosylmethionine synthetase B
S-adenosylmethionine
-
non competitive with ATP at low methionine concentration
S-adenosylmethionine
-
above 0.3 mM inhibits both high-MW and low-MW isoenzymes
S-adenosylmethionine
-
-
S-adenosylmethionine
-
noncompetitive inhibitor with respect to ATP and methionine
S-adenosylmethionine
-
more than 50% inhibition at 1 mM
S-adenosylmethionine
-
non competitive inhibition
S-adenosylmethionine
5 mM downregulates MAT2A expression
S-adenosylmethionine
-
lowers expression of MAT2A and MAT2beta
S-carbamylcysteine
-
competitive with methionine
S-nitrosoglutathione
-
inhibits S-adenosylmethionine sinthetase activity
S-nitrosoglutathione
-
inactivates MATI/III by 70%
S-nitrosoglutathione monoethyl ester
-
inactivates
S-nitrosylated glutathione
-
rapid and dose-dependent loss of enzymatic activity of MAT I/III
S-Trifluoromethyl-L-homocysteine
-
-
seleno-L-methionine
-
-
SIN-1
-
rapid and dose-dependent loss of enzymatic activity of MAT I/III
Sodium diphosphate
-
-
spermidine
15-34% inhibition with 5 mM; 15-34% inhibition with 5 mM; 15-34% inhibition with 5 mM
spermine
30-40% inhibition with 5 mM; 30-40% inhibition with 5 mM; 30-40% inhibition with 5 mM
Tetrapolyphosphate
-
; 10 mM, 40% inhibition, S-adenosylmethionine synthetase B; 10 mM, 50% inhibition, S-adenosylmethionine synthetase A
Tetrapolyphosphate
-
-
tripolyphosphate
-
-
tripolyphosphate
-
1.0 mM, 57% inhibition, S-adenosylmethionine synthetase A; 1.0 mM, 62% inhibition, S-adenosylmethionine synthetase B
tripolyphosphate
-
-
tripolyphosphate
-
competitive with ATP and non competitive with L-methionine
tripolyphosphate
-
activation or inhibition, depending on isoenzyme, S-adenosylmethionine and tripolyphosphate concentration
tripolyphosphate
-
competitive with ATP
tripolyphosphate
-
-
tripolyphosphate
strong inhibitor; strong inhibitor; strong inhibitor
tripolyphosphate
-
competitive with ATP; non competitive with L-methionine
Uric acid
10 mM, 45.6% inhibition
xanthine
10 mM, 35.4% inhibition
Zn2+
-
22.17% residual activity at 5 mM
Mn2+
-
73.49% residual activity at 5 mM
additional information
-
S-adenosyl(5')-3-methylthiopropylamine does not inhibit
-
additional information
-
overview of the regulatory properties, effect of L-methionine analogues and influence of L-methionine concentration on activating and inhibiting effects, effect of tripolyphosphate and p-hydroxymercuribenzoate
-
additional information
addition of reducing agents has no effect; addition of reducing agents has no effect; addition of reducing agents has no effect
-
additional information
-
MAT is inactivated after 6 h of incubation in hypoxia (3% O2) in rat hepatocytes, prevented by NG-monomethyl-L-arginine methyl ester. Hepatic MAT s a sensible target for free radicals in vivo
-
additional information
-
reactive oxygen and nitrogen species induce the inactivation of MAT I/III
-
additional information
-
no inhibition with cycloleucine, L-homocysteine, L-norleucine, L-cis-2-amino-4-methoxy-3-butenoic acid, S-adenosylhomocysteine, 5'-methylthioadenosine, sinefungin
-
additional information
not inhibitory: (R)-methioninol, 1,3,7-trimethyluric acid, 6-methylpurine
-
additional information
-
no effect on activity at 0.1 mM Ni2+
-
additional information
-
overexpression of yeast AdoMet synthase plus cap guanine-N7 methyltransferase affords greater resistance to sinefungin than either enzyme alone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
tripolyphosphatase activity stimulated by preincubation with ATP and methionine
cycloheximide
-
cycloheximide inhibition of protein synthesis increases isozyme MAT2 mRNA level in the logarithmic phase only, an indication that the gene is regulated in promastigotes at the posttranscriptional level by protein factors that targets the transcript for degradation
Dimethylsulfoxide
-
activates isoform from kidney and isoform MAT-III from liver
Dimethylsulfoxide
-
activates alpha and beta isoenzymes from liver
Dimethylsulfoxide
-
activates the beta isozyme from liver 13-15fold; weak activation of the alpha isozyme from liver
dithiothreitol
-
required for alpha and beta isoenzymes activity, not required for gamma enzyme
E2F1
-
present continually in the MAT2A promoter during liver regeneration
-
E2F3
-
present continually in the MAT2A promoter during liver regeneration
-
E2F4
-
present continually in the MAT2A promoter during liver regeneration
-
Epidermal growth factor
-
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
Epidermal growth factor
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
forskolin
-
induction of enzyme in organ cell culture
glycerol
-
activates rat liver isoenzymes alpha and beta
insulin-like growth factor 1
-
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
-
insulin-like growth factor 1
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
-
isoproterenol
-
induction of enzyme in organ cell culture
L-methionine
17% increase is observed at 60 mM L-methionine; 17% increase of activity is observed at 60 mM L-methionine
leptin
-
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
-
leptin
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
-
leptin
-
induces the expression of MAT2A and MAT2beta
-
methanol
-
53.26% increased yield of S-adenosyl-L-methionine at 1.0% methanol
n-heptane
-
53.26% increased yield of S-adenosyl-L-methionine at 1.0% n-heptane
norepinephrine
-
induction of enzyme in organ cell culture
S-adenosylmethionine
-
activation of rat liver MAT-III
S-adenosylmethionine
-
activates the tripolyphosphatase activity of A isoform
S-adenosylmethionine
-
below 0.3 mM activates low-MW isoenzyme
S-adenosylmethionine
-
enhances tripolyphosphatase activity
S-adenosylmethionine
-
nonessential activator of tripolyphosphatase activity in the range of 0.005-0.100 mM
SH-reagents
-
liver enzyme: requirement, tumor enzyme: no requirement
-
sorbitol
-
53.26% increased yield of S-adenosyl-L-methionine at 1.2% sorbitol
Sp1
-
binding of Sp1 to the MAT2A promoter is essential for the transcriptional up-regulation of the gene
-
tripolyphosphates
-
activation or inhibition, depending on isoenzyme, S-adenosylmethionine and tripolyphosphate concentration
Tumor necrosis factor alpha
-
induces expression of variant 1 (but not variant 2) MAT2beta
-
methionine
-
stimulation of activity demonstrated in vivo. Tripolyphosphatase activity stimulated by preincubation with ATP and methionine
additional information
-
no requirement for reducing agents
-
additional information
-
no effect with ADP and methionine or S-adenosylmethionine
-
additional information
salt stress induces the enzyme, differential effects on betaine and lignin biosynthesis, overview; salt stress induces the enzyme, differential effects on betaine and lignin biosynthesis, overview; salt stress induces the enzyme, differential effects on betaine and lignin biosynthesis, overview; salt stress induces the enzyme, differential effects on betaine and lignin biosynthesis, overview
-
additional information
-
methanol induces enzyme expression and S-adenosyl-L-methionine production, while glycerol does not
-
additional information
cell methionine and S-adenosylmethionine contents increase in response to hyperoxia in SAE and A549 cells, enzyme activity increases by 2fold within 5 days, S-adenosylmethionine content by 5fold, overview
-
additional information
-
fasting for 10-16 h increases expression and activity of isozymes MAT I and MAT III, effects on methionine/S-adenosyl-L-methionine metabolism, overview
-
additional information
-
lysine enhances methionine content by modulating the expression of S-adenosylmethionine synthase, overview
-
additional information
-
no significant effect in the presence of n-dodecane
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
ATP
-
beta form from liver
0.005
ATP
-
alpha form from liver
0.0145
ATP
pH 8.0, 65C, cosubstrate: L-methionine
0.026
ATP
-
G6 mutant, S-adenosylmethionine synthesis
0.045
ATP
-
RLL and G8 mutants, S-adenosylmethionine synthesis
0.05
ATP
-
isoenzyme A
0.05
ATP
-
-
0.0592
ATP
pH 8.0, 65C, cosubstrate: L-ethionine
0.065
ATP
-
S-adenosylmethionine synthetase A
0.0686
ATP
pH 8.0, 37C, cosubstrate: L-methionine
0.069
ATP
-
G7 mutants, S-adenosylmethionine synthesis
0.073
ATP
-
wild-type S-adenosylmethionine synthesis
0.076
ATP
37C, pH 8.2
0.08
ATP
-
-
0.083
ATP
-
wild-type, pH 8.0
0.087
ATP
-
G5 mutant S-adenosylmethionine synthesis
0.0969
ATP
pH 8.0, 37C, cosubstrate: L-ethionine
0.1
ATP
-
mutant W387F/Y170W, 55C; mutant W387F/Y226W, 55C
0.11
ATP
-
mutant W387F, 55C; mutant W387F/Y371W, 55C; mutant W387F/Y72W, 55C
0.115
ATP
pH 8.0, 80C
0.13
ATP
-
mutant D107C, pH 8.0; mutant G105C, pH 8.0
0.13
ATP
-
mutant W387F/Y120W, 55C
0.15
ATP
-
isoenzyme B
0.156
ATP
-
S-adenosylmethionine synthetase B
0.18
ATP
-
mutant G105R1, pH 8.0
0.18
ATP
-
mutant W387F/Y49W, 55C
0.19
ATP
-
mutant W387F/Y255W, 55C; wild-type, 55C
0.2
ATP
-
mutant W387F/Y233W, 55C; mutant W387F/Y267W, 55C
0.21
ATP
-
mutant W387F/Y85W, 55C
0.22
ATP
-
saturated with KCl
0.22
ATP
-
mutant W387F/Y323W, 55C; mutant W387F/Y344W, 55C
0.24
ATP
-
mutant W387F/Y273W, 55C
0.25
ATP
-
pH 8.0, 58C
0.33
ATP
-
pH 8.0, 37C
0.34
ATP
pH 8.0, 37C
0.493
ATP
mutant C35S, presence of dithiothreitol
0.53
ATP
wild-type, presence of glutathione
0.588
ATP
wild-type, presence of dithiothreitol
0.631
ATP
-
at pH 8.0 and 35C
0.778
ATP
mutant C35S, presence of glutathione
0.92
ATP
in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37C
2.54
ATP
mutant C61S, presence of glutathione
3.25
ATP
mutant C61S, presence of dithiothreitol
31
ATP
-
-
3.5
D-methionine
-
-
1.4
ITP
-
pH 8.0, 58C
0.0056
L-ethionine
pH 8.0, 37C
0.007
L-ethionine
pH 8.0, 65C
0.74
L-ethionine
-
-
0.0023
L-methionine
pH 8.0, 37C
0.0028
L-methionine
pH 8.0, 65C
0.0029
L-methionine
-
-
0.003
L-methionine
-
-
0.0061
L-methionine
-
pH 7.0, 37C
0.0075
L-methionine
-
erythrocyte extract, alpha and beta subunit
0.01
L-methionine
-
isoenzyme A; S-adenosylmethionine synthetase A
0.01
L-methionine
-
-
0.0125
L-methionine
-
erythrocyte extract, alpha subunit
0.015
L-methionine
-
endogenous MAT II
0.015
L-methionine
-
-
0.016
L-methionine
-
alpha2-transfected MAT II, two kinetic forms
0.017
L-methionine
-
alpha form from liver
0.02
L-methionine
-
isoenzyme B
0.02
L-methionine
-
recombinant MAT II co-expressing alpha2 and beta subunits
0.022 - 0.024
L-methionine
-
ro subunit
0.022
L-methionine
-
crude extract
0.022
L-methionine
one kinetic form of alpha-two subunit in the presence of beta subunit
0.024
L-methionine
-
S-adenosylmethionine synthetase B
0.024
L-methionine
-
wild-type
0.03 - 0.038
L-methionine
-
one kinetic form of alpha subunit in the presence of beta subunit
0.03
L-methionine
-
mutant D249N, pH 8.0
0.031
L-methionine
pH 8.0, 80C
0.036
L-methionine
-
mutant D166N, pH 8.0
0.038
L-methionine
-
mutant D19N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.04
L-methionine
-
wild-type, pH 8.0
0.041
L-methionine
-
MAT-I isoenzyme
0.041
L-methionine
-
mutant K280A, pH 8.0
0.045
L-methionine
-
mutant D121N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.05
L-methionine
-
mutant D249N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.06
L-methionine
-
uninduced E. coli NM522 strain extract alpha subunit at low L-methionine concentrations
0.06 - 0.1
L-methionine
alpha-two subunit
0.065 - 0.08
L-methionine
-
alpha subunit at low L-methionine concentrations
0.074
L-methionine
-
mutant K280A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.075
L-methionine
-
alpha2-transfected MAT II, two kinetic forms
0.076
L-methionine
one kinetic form of alpha-two subunit in the presence of beta subunit
0.08 - 0.09
L-methionine
-
alpha subunit at high L-methionine concentrations. Also one kinetic form of alpha subunit in the presence of beta subunit
0.08
L-methionine
-
induced E. coli NM522 strain extract alpha subunit at low L-methionine concentrations and uninduced E. coli NM522 strain extract alpha subunit at high L-methionine concentrations
0.08
L-methionine
-
S283T mutant
0.088
L-methionine
-
Q113A mutant, S-adenosylmethionine synthesis
0.092
L-methionine
-
wild-type, S-adenosylmethionine synthesis
0.096
L-methionine
-
pH 8.2, 37C
0.11
L-methionine
-
wild-type, pH 8.0
0.11
L-methionine
pH 8.0, 37C
0.12
L-methionine
-
pH 8.0, 37C
0.13
L-methionine
-
mutant W387F/Y323W, 55C; mutant W387F/Y72W, 55C
0.137
L-methionine
-
mutant D282N, presence of 0.05 mM S-adenosyl methionine, pH 8.0; mutant H17N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.14
L-methionine
-
pH 8.0, 58C
0.141
L-methionine
-
mutant D282N, pH 8.0
0.147
L-methionine
-
mutant D166N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.17
L-methionine
-
mutant K256A, pH 8.0; mutant K256A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.176
L-methionine
-
mutant H17A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.18
L-methionine
-
mutant D107R1, pH 8.0
0.19
L-methionine
-
mutant D107R1, pH 8.0
0.2
L-methionine
-
induced E. coli NM522 strain extract alpha subunit at high L-methionine concentrations
0.215
L-methionine
-
MAT-III isoenzyme
0.22
L-methionine
-
wild-type
0.23
L-methionine
-
RLL mutant, S-adenosylmethionine synthesis
0.24
L-methionine
-
-
0.25
L-methionine
-
mutant W387F/Y371W, 55C
0.26
L-methionine
in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37C
0.287
L-methionine
-
wild-type, presence of 0.05 mM S-adenosyl methionine, pH 8.0
0.288
L-methionine
37C, pH 8.2
0.29
L-methionine
-
mutant D107C, pH 8.0
0.3
L-methionine
-
saturated with KCl
0.3
L-methionine
-
G6 mutant, S-adenosylmethionine synthesis
0.3
L-methionine
-
mutant W387F/Y226W, 55C; mutant W387F/Y273W, 55C
0.31
L-methionine
-
mutant W387F, 55C; wild-type, 55C
0.33
L-methionine
-
mutant W387F/Y344W, 55C
0.45
L-methionine
-
mutant G105C, pH 8.0
0.45
L-methionine
-
mutant W387F/Y267W, 55C
0.47
L-methionine
-
mutant W387F/Y233W, 55C
0.49
L-methionine
-
G7 mutant, S-adenosylmethionine synthesis
0.5
L-methionine
-
mutant W387F/Y255W, 55C
0.527
L-methionine
-
at pH 8.0 and 35C
0.54
L-methionine
-
mutant W387F/Y120W, 55C
0.57
L-methionine
-
mutant W387F/Y85W, 55C
0.62
L-methionine
-
G8 mutant, S-adenosylmethionine synthesis
0.66
L-methionine
-
mutant W387F/Y49W, 55C
0.75
L-methionine
-
mutant G105R1, pH 8.0
0.77
L-methionine
-
G5 mutant, S-adenosylmethionine synthesis
1
L-methionine
-
mutant W387F/Y170W, 55C
1.1
L-methionine
-
-
3.3
L-methionine
-
-
2.6
L-methionine methyl esther
-
-
0.0083
methionine
-
MAT-II isoenzyme
0.222
methionine
mutant C35S, presence of dithiothreitol
0.246
methionine
wild-type, presence of dithiothreitol
0.4
methionine
-
-
0.449
methionine
mutant C35S, presence of glutathione
0.5
methionine
-
beta form from liver
0.756
methionine
mutant C61S, presence of dithiothreitol
0.794
methionine
mutant C61S, presence of glutathione
1.12
methionine
wild-type, presence of glutathione
0.006
Mg2+
-
alpha form from liver
0.007
Mg2+
-
beta form from liver
0.0013
tripolyphosphate
-
wild type, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.0015
tripolyphosphate
-
G7 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.0016
tripolyphosphate
-
G8 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.003
tripolyphosphate
-
wild type, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.0032
tripolyphosphate
-
G6 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.0053
tripolyphosphate
-
G5 mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.008
tripolyphosphate
-
G8 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.011
tripolyphosphate
-
G6 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.014
tripolyphosphate
-
RLL mutant, tripolyphosphatase activity, in absence of S-adenosylmethionine
0.015
tripolyphosphate
-
G7 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.024
tripolyphosphate
-
G5 mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.026
tripolyphosphate
-
RLL mutant, tripolyphosphatase activity, in the presence of 0.1 mM of S-adenosylmethionine
0.3
MgATP2-
-
-
additional information
additional information
-
high performance liquid chromatography assay method using catechol-O-methyltransferase-coupled fluorometric detection, negative cooperativity of enzyme with Hill coefficinet of 0.5
-
additional information
additional information
-
different isoforms of MAT differ in kinetic and regulatory properties, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000883
ATP
Leishmania infantum
-
-
0.0328
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C, cosubstrate: L-methionine
0.041
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C, cosubstrate: L-ethionine
0.047
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C, cosubstrate: L-methionine
0.052
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C, cosubstrate: L-ethionine
7.5
ATP
Pyrococcus furiosus
Q8TZW1
pH 8.0, 80C
0.039
L-ethionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C
0.05
L-ethionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C
0.0343
L-methionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C
0.049
L-methionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C
0.23
L-methionine
Escherichia coli
-
mutant D107R, pH 8.0
0.93
L-methionine
Mycobacterium smegmatis
Q7WYN1
37C, pH 8.2
1
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y49W, 55C
1.4
L-methionine
Escherichia coli
-
mutant G105R, pH 8.0
1.46
L-methionine
Methanocaldococcus jannaschii
-
wild-type, 55C
1.5
L-methionine
Escherichia coli
-
wild-type, pH 8.0
1.54
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y273W, 55C
1.6
L-methionine
Escherichia coli
-
mutant D107C, pH 8.0; mutant G105C, pH 8.0
1.62
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y323W, 55C; mutant W387F/Y72W, 55C
1.85
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F, 55C
2.31
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y267W, 55C
2.39
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y170W, 55C; mutant W387F/Y255W, 55C
2.77
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y85W, 55C
2.85
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y344W, 55C
3.31
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y120W, 55C
4
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y371W, 55C
5.08
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y226W, 55C
7.24
L-methionine
Methanocaldococcus jannaschii
-
mutant W387F/Y233W, 55C
7.5
L-methionine
Pyrococcus furiosus
Q8TZW1
pH 8.0, 80C
0.000000367
S-adenosylmethionine
Escherichia coli
-
RLL mutant, S-adenosylmethionine synthesis
0.00000045
S-adenosylmethionine
Escherichia coli
-
G6 mutant, S-adenosylmethionine synthesis
0.000000667
S-adenosylmethionine
Escherichia coli
-
G8 mutant, S-adenosylmethionine synthesis
0.00000217
S-adenosylmethionine
Escherichia coli
-
G5 mutant, S-adenosylmethionine synthesis
0.000012
S-adenosylmethionine
Escherichia coli
-
G7 mutant, S-adenosylmethionine synthesis
0.0000883
S-adenosylmethionine
Leishmania infantum
-
-
0.000417
S-adenosylmethionine
Escherichia coli
-
wild-type, S-adenosylmethionine synthesis
0.032
S-adenosylmethionine
Leishmania donovani
-
S-adenosylmethionine synthesis activity
0.583
S-adenosylmethionine
Rattus norvegicus
-
S-adenosylmethionine synthesis
0.000000217
tripolyphosphate
Escherichia coli
-
G8 mutant, tripolyphosphatase activity
0.000000617
tripolyphosphate
Escherichia coli
-
G6 mutant, tripolyphosphatase activity
0.000000633
tripolyphosphate
Escherichia coli
-
G5 mutant, tripolyphosphatase activity
0.00000122
tripolyphosphate
Escherichia coli
-
RLL and G7 mutants, tripolyphosphatase activity
0.00000167
tripolyphosphate
Escherichia coli
-
wild-type, tripolyphosphatase activity
0.004
tripolyphosphate
Leishmania donovani
-
tripolyphosphase activity
0.125
tripolyphosphate
Rattus norvegicus
-
tripolyphosphatase activity
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C, cosubstrate: L-ethionine
4
0.48
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C, cosubstrate: L-methionine
4
0.87
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C, cosubstrate: L-ethionine
4
3.23
ATP
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C, cosubstrate: L-methionine
4
65.2
ATP
Pyrococcus furiosus
Q8TZW1
pH 8.0, 80C
4
6.95
L-ethionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C
1447
7.12
L-ethionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C
1447
14.92
L-methionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 37C
88
17.37
L-methionine
Sulfolobus solfataricus
Q980S9
pH 8.0, 65C
88
242
L-methionine
Pyrococcus furiosus
Q8TZW1
pH 8.0, 80C
88
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
8-Azaguanine
37C, pH 8.2
0.8
ATP
-
noncompetitive inhibition at 0.5-5 mM ATP concentrations
3.7
Azathioprine
37C, pH 8.2
3.6
cycloleucine
-
pH 8.2, 37C
17
cycloleucine
-
-
0.4
D-methionine
-
-
0.000002
diimidotriphosphate
-
pH 8.0
0.3
diphosphate
-
inhibition with respect to ATP
0.35
diphosphate
-
inhibition with respect to L-methionine
0.71
DL-Ethionine
-
-
0.0031
L-2-Amino-4-methoxy-cis-but-3-enoic acid
-
isoenzyme II
0.0063
L-2-Amino-4-methoxy-cis-but-3-enoic acid
-
isoenzyme I
0.0057
L-2-Amino-4-methylthio-cis-but-3-enoic acid
-
isoenzyme II
250
Na+
-
in presence of Mg2+
0.05
S-adenosylmethionine
-
inhibits the A isoform; S-adenosylmethionine synthetase A
0.24
S-adenosylmethionine
-
-
0.8
S-adenosylmethionine
-
ATP concentrations of 0.5-5 mM
4
S-adenosylmethionine
-
noncompetitive inhibition at 0.5-5 mM L-methionine concentrations
4
S-adenosylmethionine
-
L-methionine concentrations of 0.5-5 mM
0.51
seleno-L-methionine
-
-
1.6
Sodium diphosphate
-
-
0.18
Tetrapolyphosphate
-
-
0.035
tripolyphosphate
-
0.05
tripolyphosphate
-
-
0.2
tripolyphosphate
-
inhibition with respect to L-methionine
0.25
tripolyphosphate
-
inhibition with respect to ATP
0.021
L-2-Amino-4-methylthio-cis-but-3-enoic acid
-
isoenzyme I
additional information
additional information
-
Ki values for several phosphonate analogues and nucleotides
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000019
1-(3-(2-ethoxyphenyl)ureidoacetyl)-4-(2-methyl-5-nitrophenyl)semicarbazide
Escherichia coli
-
pH 8.0, 25C
0.0000069
1-(4-chloro-2-nitrophenyl)-3-(4-sulfamoylphenyl)-urea
Escherichia coli
-
pH 8.0, 25C
0.287
Cu2+
Rattus norvegicus
P13444
isozyme subunit MATalpha2, in the absence of dithiothreitol
0.748
Cu2+
Rattus norvegicus
P13444
isozyme subunit MATalpha2, in the presence of dithiothreitol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0002
-
activity Peak II, adult erythrocytes
0.001
-
brain
0.0011
-
muscle
0.0041
-
pancreas
0.0042
-
intestine
0.0061
-
kidney
0.039
-
MAT I
0.0431
-
liver
0.058
-
tripolyphosphase activity
0.065
-
S-adenosylmethionine synthetase B
0.096
-
glutathione/glutathione disulfide-refolded MAT III
0.098
-
MAT III
0.1
-
glutathione/glutathione disulfide-refolded MAT I
0.109
purified recombinant His-tagged isozyme SAMS1
0.11
-
dithiothreitol-refolded MAT III
0.138
-
S-adenosylmethionine synthetase A
0.2
-
S-adenosylmethionine synthesis activity
0.28
-
low-MW isozyme
0.94
-
pH 8.0, 37C
3
-
beta isoenzyme from liver
4.61
-
high-MW isozyme
6.42
-
crude extract, at 35C
7.5
-
alpha isoenzyme from liver
11
-
isoenzyme II
12.2
-
-
12.4
-
-
18.7
-
isoenzyme I
23.83
-
after 3.71fold purification, at 35C
32.75
-
beta form from liver
39
-
gamma isoenzyme from liver
66
-
mutant D121N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
78.24
-
alpha form from liver
108
-
mutant D166N, pH 8.0; mutant D19N, presence of 0.05 mM S-adenosyl methionine, pH 8.0; mutant D282N, pH 8.0
138
-
mutant D249N, pH 8.0
210
-
mutant H17A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
216
-
pH 7.0, 37C
222
-
wild-type, pH 8.0
240
-
mutant D282N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
252
-
mutant K256A, pH 8.0; mutant K256A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
318
-
mutant K280A, pH 8.0
330
-
mutant D249N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
720
-
mutant K280A, presence of 0.05 mM S-adenosyl methionine, pH 8.0
792
-
mutant D166N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
960
-
mutant H17N, presence of 0.05 mM S-adenosyl methionine, pH 8.0
3000
-
wild-type, presence of 0.05 mM S-adenosyl methionine, pH 8.0
4400
-
pH 8.2, 37C
31500
mutant C61S, presence of glutathione
32700
mutant C35S, presence of glutathione
69070
mutant C61S, presence of dithiothreitol
94470
mutant C35S, presence of dithiothreitol
95800
wild-type, presence of glutathione
110000
wild-type, presence of dithiothreitol
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
different values in refolding and purification process
additional information
-
additional information
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
assay at
7 - 8.3
three isoenzymes; three isoenzymes; three isoenzymes
7.4
-
assay at
7.4
assay at
7.5 - 9.5
-
glutathione/glutathione disulfide-refolded MAT I
7.7 - 8.8
-
MAT III, MAT I and dithiothreitol-refolded MAT III
8
-
assay at
8.1
-
; S-adenosylmethionine synthetase A; S-adenosylmethionine synthetase B
8.2
-
assay at
8.5 - 10
-
glutathione/glutathione disulfide-refolded MAT III
9
-
slight variation in activity between 8 and 10
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
more than 60% of maximum activity within
7 - 9
half of the maximal activity at pH 7 and 9
7.2 - 9.3
-
50% of maximal activity at pH 7.2 and at pH 9.3, S-adenosylmethionine synthetase A; 50% of maximal activity at pH 7.2 and at pH 9.3, S-adenosylmethionine synthetase B; about 50% of activity maximum at pH 7.2 and 9.3
7.5 - 8.5
-
-
7.5 - 9.5
-
about 70-80% of maximal activity at pH 7.5 and 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
assay at; assay at; assay at
37
-
assay at
37
-
assay at
70
-
optimal growth temperature for Methanococcus jannaschii: 87C
90
-
; S-adenosylmethionine synthetase A
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
50% of maximum activity
70 - 105
70C: about 55% of maximal activity, 105C: about 60% of maximal activity
75 - 110
-
50% of maximal activity at 75C and at 110C; about 50% of activity maximum at 75C and 110C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
-
isoelectric focusing
4.82
sequence calculation
5.52
calculated from sequence
6.25
-
calculated from amino acid sequence
7.2
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
both subcutaneous fat content and intramusclular fat content are higher in obese than in lean pigs. MAT2beta mRNA abundance is lower in both subcutaneous adipose tissue and skeletal muscle in obese pigs compared with lean pigs
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
L1210 cell line, two isoenzymes
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
hepatocellular carcinoma, MAT1A is replaced by MAT2A
Manually annotated by BRENDA team
regulatory subunit MAT2beta is expressed at a higher level in liver and duodenum, followed by the stomach, fat and longissinus dorsi muscle
Manually annotated by BRENDA team
lung epithelial isoform of MAT 2A
Manually annotated by BRENDA team
regulatory subunit MAT2beta is expressed at a higher level in liver and duodenum, followed by the stomach, fat and longissinus dorsi muscle
Manually annotated by BRENDA team
maximum mRNA accumulation is attained in the evening
Manually annotated by BRENDA team
-
mainly MAT2beta variant 2
Manually annotated by BRENDA team
-
in cultured hepatocytes MAT1A expression falls and MAT2A is induced when S-adenosyl-L-methionine level falls, which can be prevented by exogenous S-adenosyl-L-methionine
Manually annotated by BRENDA team
-
adult quiescent hepatocyte
Manually annotated by BRENDA team
-
leukemia promyelotic cells
Manually annotated by BRENDA team
Jurkat cell isoform of MAT 2A
Manually annotated by BRENDA team
-
gamma isoenzyme in kidney enzyme
Manually annotated by BRENDA team
-
MAT2beta variant 1 and 2
Manually annotated by BRENDA team
-
two isofunctional forms with different Km values
Manually annotated by BRENDA team
-
alpha and beta isozymes
Manually annotated by BRENDA team
-
alpha and beta isozymes; two isofunctional forms with different Km values
Manually annotated by BRENDA team
-
MAT I/III isozymes
Manually annotated by BRENDA team
-
three isofunctional forms
Manually annotated by BRENDA team
-
predominant expression of MAT1A, induction of MAT2A during periods of rapid growth and dedifferentiation
Manually annotated by BRENDA team
-
predominant expression of MAT1A, induction of MAT2A during periods of rapid growth and dedifferentiaition; predominant expression of MAT1A, induction of MAT2A during periods of rapid growth and dedifferentiation
Manually annotated by BRENDA team
-
expression of MAT1A, a marker for differentiated liver, MAT1A progressively replaces MAT2A, which is mainly expressed in fetal liver
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
expression of isoform MAT1A in the adult liver. During hepatic de-differentiation, the switch between MAT1A and MAT2A coincides with an increase in HuR and AUF1 expression. S-adenosylmethionine treatment alters this homeostasis by shifting the balance of AUF1 and methyl-HuR/HuR. Similar temporal distribution and functional link between HuR, methyl-HuR, AUF1, and MAT1A and MAT2A during fetal liver development
Manually annotated by BRENDA team
regulatory subunit MAT2beta is expressed at a higher level in liver and duodenum, followed by the stomach, fat and longissinus dorsi muscle
Manually annotated by BRENDA team
regulatory subunit MAT2beta is expressed at a higher level in liver and duodenum, followed by the stomach, fat and longissinus dorsi muscle. MAT2beta mRNA abundance is lower in both subcutaneous adipose tissue and skeletal muscle in obese pigs compared with lean pigs. MAT II beta protein content is lower in skeletal muscle in obese than in lean pigs
Manually annotated by BRENDA team
lung epithelial isoform of MAT 2A, epithelial-like and primary small airway epithelial, SAE, cells
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
from chronic leukemia cells
Manually annotated by BRENDA team
-
at night, 2.5fold increase of activity of isoform MAT II
Manually annotated by BRENDA team
Leishmania infantum LEM75
-
-
-
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
greatest abundance
Manually annotated by BRENDA team
-
green of 14-days old of seedlings
Manually annotated by BRENDA team
-
mainly MAT2beta variant 2
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
isoforms MAT2AandMAT2beta are induced in culture-activated primary hepatic stellate cells and hepatic stellate cells from 10-day bile duct ligated rat livers. Hepatic stellate cell activation leads to a decline in intracellular S-adenosylmethionine and methyhthioadenosine levels, a drop in the S-adenosylmethionine/S-adenosylhomocysteine ratio, and global DNA hypomethylation. The decrease in S-adenosylmethionen levels is associated with lower MATII activity during activation
Manually annotated by BRENDA team
regulatory subunit MAT2beta is expressed at a higher level in liver and duodenum, followed by the stomach, fat and longissinus dorsi muscle
Manually annotated by BRENDA team
T helper CD4+ lymphocyte
Manually annotated by BRENDA team
-
mainly MAT2beta variant 2
Manually annotated by BRENDA team
-
MAT2beta variant 1 and 2
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
additional information
-
isoenzyme MAT-II present in all tissues
Manually annotated by BRENDA team
additional information
isozyme expression pattern in plant tissues, overview; isozyme expression pattern in plant tissues, overview; isozyme expression pattern in plant tissues, overview; isozyme expression pattern in plant tissues, overview
Manually annotated by BRENDA team
additional information
-
expression in all cell types and plant organs, with preferential accumulation in lignified tissues
Manually annotated by BRENDA team
additional information
-
development of a feeding strategy during the production phase for enhancing the enzymatic synthesis of S-adenosyl-L-methionine, overview
Manually annotated by BRENDA team
additional information
-
almost no expression of MAT2beta variant 1 or 2 in bone marrow, trachea, salivary gland, uterus, adult liver, and placenta
Manually annotated by BRENDA team
additional information
-
development of a feeding strategy during the production phase for enhancing the enzymatic synthesis of S-adenosyl-L-methionine, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform MAT I, presence of two partially overlapping areas at the C-terminal end of the protein involved both in cytoplasmic retention and nuclear localization
Manually annotated by BRENDA team
-
; S-adenosylmethionine synthetase A; S-adenosylmethionine synthetase B
Manually annotated by BRENDA team
-
isoform MAT I, in extrahepatic tissues, the protein colocalizes with nuclear matrix markers. Presence of two partially overlapping areas at the C-terminal end of the protein involved both in cytoplasmic retention and nuclear localization. Neither nuclear localization nor matrix binding requires activity. Nuclear accumulation of the active enzyme only correlates with histone H3K27 trimethylation among the epigenetic modifications evaluated
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia pseudomallei (strain K96243)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium avium (strain 104)
Mycobacterium marinum (strain ATCC BAA-535 / M)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32500
-
beta subunit, gel filtration
639059
38000 - 39000
MAT II beta subunit, gel filtration
639070
42000
SDS-PAGE
684597
42560
SAMS 3, gel filtration
639063
43000
SAMS 2, gel filtration
639063
43050
SAMS 1, gel filtration
639063
45000
SDS-PAGE
686475
45000
SDS-PAGE
686475
45000
SDS-PAGE
686475
46000
2D-PAGE
639077
48000
-
monomer, gel filtration and immunoblotting
639071
48000
-
MAT II, gel filtration
639078
49000
-
native MAT-II, gel filtration
639075
50500
-
calculated from amino acid sequence
685831
51000
-
expression of the alpha subunit in E. coli, gel filtration
639060
53000
-
alpha subunit, gel filtration
639059
53000
-
expression of the alpha subunit in E. coli, gel filtration
639060
60000
-
isoenzyme ro, Peak I, gel filtration
639059
75000
-
isoenzyme B, gel filtration; S-adenosylmethionine synthetase B, gel filtration
639048
86000
-
recombinant enzyme, gel filtration
639074
89130
-
glutathione/glutathione disulfide-refolded MAT III, gel filtration
639071
90000
gel filtration
728983
92700
-
dithiothreitol-refolded MAT III, gel filtration
639071
92700
gel filtration
659298
97000
-
MAT-III, gel filtration
639043
97000
-
-
639044
100000
-
beta isoenzyme from liver, gel filtration
639058
110000
-
low-MW isoenzyme, gel filtration
639053
110000
-
forms I and II, gel filtration
639055
110000
-
MAT III, gel filtration
639071
110000
isozyme MAT III, gel filtration
686024
120000
-
MAT-II, isolated from kidney and liver, gel filtration
639043
120000
-
-
639044
145000
-
gel filtration
639046
160000
-
beta isoenzyme from liver, gel filtration
639054
160000
-
gel filtration
639057
180000
-
-
639045
180000
-
isoenzyme A, gel filtration; S-adenosylmethionine synthetase A, gel filtration
639048
180000
-
X-ray crystallography
639049
180000
-
gel filtration
639056
180000
gel filtration
685392
185000
-
equilibrium sedimentation studies
639052
190000
-
gamma isoenzyme from kidney, gel filtration
639054
194900
-
glutathione/glutathione disulfide-refolded MAT I, gel filtration
639071
194900
gel filtration
659298
200000
-
alpha isoenzyme from liver, gel filtration
639058
200000
isozyme MAT I, gel filtration; isozyme MAT II, gel filtration
686024
208000
-
MAT-I, gel filtration
639043
208000
-
-
639044
210000
-
high-MW isoenzyme, gel filtration
639053
210000
-
alpha isoenzyme, gel filtration
639054
210000
-
MAT I
639071
249000
-
recombinant MAT-II, gel filtration
639075
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43000
?
-
x * 48000 + x * 38000, SDS-PAGE
?
-
ro subunit may exist in a monomeric or polymeric form
?
-
x * 44800, calculated
?
x * 43500, recombinant enzyme, SDS-PAGE
?
x * 37850, sequence calculation
?
x * 43000, SDS-PAGE and calculated; x * 43000, SDS-PAGE and calculated
?
x * 37640, calculated
?
-
x * 43600, ESI-MS
dimer
-
2 * 47000, MAT-III, SDS-PAGE
dimer
-
2 * 47000, low-MW isoenzyme, SDS-PAGE
dimer
-
1 * 55000 + 1 * 60000, SDS-PAGE
dimer
-
2 * 48000, beta isoenzyme from liver, SDS-PAGE
dimer
-
recombinant enzyme is present in two different oligomeric forms that can be separated by hydrophobic chromatography and DMSO elution
dimer
-
substrate and/or reaction products promotes dimer formation
dimer
2 * 44300, analysis of association/dissociation between dimer and tetramer by gel filtration and MALDI-TOF MS
dimer
-
genes MAT1A and MAT2A encode catalytic subunits alpha1 and alpha2, respectively, the subunits differentially build the isozymes together with a regulatory beta subunit, isozyme composition, overview
dimer
isozyme MAT III
homodimer
2 * 44279, calculated from sequence; 2 * 45000, SDS-PAGE
homotetramer
4 * 45000, dimer of dimer, gel filtration
monomer
gel filtration; gel filtration; gel filtration
tetramer
-
heterotetramer with subunit composition alpha-alpha'-beta2, alpha2beta2 or alpha'2beta2, where alpha, alpha', and beta are chains of molecular weight 53000, 51000 and 38000
tetramer
-
4 * 48500, high-MW isoenzyme, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 48000, alpha isoenzyme from liver, SDS-PAGE
tetramer
-
two subunits form a spherical dimer and pairs of these dimers form a tetrameric enzyme
tetramer
-
native polyacrylamide gel electrophoresis
tetramer
-
gel filtration and native gel electrophoresis
tetramer
-
dimer of dimers, crystallization data
tetramer
4 * 44300, analysis of association/dissociation between dimer and tetramer by gel filtration and MALDI-TOF MS
tetramer
isozyme MAT I; isozyme MAT II
tetramer
-
in nuclear fractions, presence of active tetramers and monomers
monomer
-
in nuclear fractions, presence of active tetramers and monomers
additional information
-
alpha subunit from human kidney and normal or malignant lymphocytes is identical. Alpha subunit expressed in human liver. Alpha subunit is the catalytic subunit whereas beta subunit may have a regulatory function
additional information
-
alpha2 and beta subunits of MAT II associate spontaneously
additional information
; beta subunit has a regulatory function. MAT II beta subunit associates spontaneously with Escherichia coli MAT alpha subunit as well as with the recombinant human MAT II alpha-two subunit
additional information
-
study of thermal unfolding, implications for structure and oligomerization pathway
additional information
-
construction of homology model
additional information
the enzyme contains conserved sequence motifs of SAM-s proteins, such as nanopeptide 276GGGAFSGKD284 for the P-loop for ATP binding site and metal binding site with 17D and 289D for Mg2+ and 49G for K+
additional information
-
structural mapping of the the S(MK) box, conserved RNA motif in the 5'-untranslated region of the metK gene, overview
additional information
-
high stability of Methanococcus jannaschii enzyme derives largely from a tight association of its subunits in the dimer. The least stable structural elements are the C-terminal ends of beta-strands E2 and E6, and the N-terminus of E3
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hexagonal bipyramid crystals of the pyrophosphate complex grown from a solution containing phosphate, diphosphate, sulfate and Mg2+. Crystals of the ADP complex grown obtained from a solution containing phosphate, ADP, sulfate and Mg2+. Crystals of the BrADP complex obtained by a soaking method: pyrophosphate-MAT crystals obtained from a solution containing phosphate, sulfate and Mg2+, and replaced the mother liquor with a solution containing BrATP, Tris-HCl buffer, Mg+2 and ammonium sulfate
-
in complex with 5-adenylyl imido triphosphate and methionine
-
method of vapor diffusion, hexagonal bipiramid crystals in the presence of Mg2+ and diphosphate
-
quantum mechanical/molecular mechanical calculations, exploiting structures of the active crystalline enzyme, based on PDB files 1P7L and 1RG9
-
construction of a 3D-homology model. This model predicts preservation of the chain topology and three-domain organization typical of this family, locates the least stable structural elements at the flat contact surface between monomers, and shows that alterations in all three domains are required for dimer dissociation
-
in complex with inhibitor (2S,4S)-amino-4,5-epoxypentanoic acid
sitting drop method at 20C, crystallization of the enzyme in the S-adenosylmethionine bound, S-adenosylethionine bound and unbound forms
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
easily inactivated below
706910
7 - 9
-
-
706910
7.5 - 9
-
the activity of the enzyme is decreased above pH 9.0 and is inactive at pH below 7.5
685773
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
stable for several hours, if protein concentration is above 0.1 mg/ml and ionic strength is at least 50 mM
639052
30 - 40
-
enzyme activity is significantly reduced at temperatures below 30C or above 40C
685773
45
-
stable up to
706910
47 - 51
-
Tm-value, irreversible thermal denaturation
658288
70
1 h, stable
728983
80
1 h, 20% loss of activity
728983
95
half-life: 23 min
728983
99
Tm-value
728983
100
-
30 min, 90% loss of activity; more than 80% activity is retained in the presence of 10 mM ATP at 100C for 30 min. GTP, ADP, AMP and methionine do not exert any protective effect, S-adenosylmethionine synthetase A
639048
100
half-life: 5 min
728983
additional information
-
preincubation with ATP protects against thermal inactivation
639048
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
limited proteolysis experiments indicate that the proteolytic cleavage site is localized at Lys148 and that the C-terminal peptide is necessary for the integrity of the active site
significant decrease during the interval from 0-8 hr at 23C after decapitation. From here up to 72 hs post-mortem at 4C the activity remains at 60% of the initial value
-
the Ni2+-IDA agarose-immobilized synthetase exhibits 40.4% of the free enzyme activity
-
ATP, preincubation protects against thermal inactivation
-
glycerol, 10% stabilizes
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
the enzyme is fully and irreversibly unfolded in the presence of guanidinium chloride. Unfolding of this dimeric protein is a three-state process in which a dimeric intermediate can be identified. The less stable secondary structural elements of the protein are the C-terminal ends of beta-strands E2 and E6
guanidine-HCl
midpoint transition is 3.2 M
guanidine-HCl
-
the enzyme is fully and irreversibly unfolded in the presence of guanidinium chloride. Unfolding of this dimeric protein is a three-state process in which a dimeric intermediate can be identified. The less stable secondary structural elements of the protein are the C-terminal ends of beta-strands E2 and E6
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2C, stable for at least 2 months
-
-70C, 5 mg/ml enzyme concentration
-
-70C, less than 10% loss of activity after 3 months
-
0C, 50 mM Tris/HCl, pH 7.8, 20% v/v glycerol, 0.2 mM DTT, 0.1 mM EDTA, 10 mM MgCl2, 0.1 M KCl, partially purified liver enzymes stable for at least 1 month
-
-20C, partially purified isoenzymes, 10 mM Tris/HCl, pH 8, stable for 4 weeks
-
-20C, pH 8, 10 mM Tris/HCl buffer, partially purified S-adenosylmethionine synthetase A is stable for four weeks
-
-20C, pH 8, 10 mM Tris/HCl buffer, partially purified S-adenosylmethionine synthetase B is stable for four weeks
-
4C, isoenzyme A and B are spontaneously inactivated in 1 month and 1 week, respectively, in presence of glycerol stability increases up to 90%
-
4C, S-adenosylmethionine synthetase is spontaneously inactivated in 1 month, S-adenosylmethionine synthetase A
-
4C, S-adenosylmethionine synthetase is spontaneously inactivated in 1 week
-
are stable in buffer A at
-
-70C, 63% loss of activity after 3 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombiant His-tagged isozyme SAMS1 from Escherichia coli strain M15
Ni-NTA column chromatography
partial
-
Ni-NTA column chromatography
-
method that includes ammonium sulfate fraction, phenyl-Sepharose HR and hydroxylapetite CHT-1 chromatographies and amminohexyl-Sepharose anion exchange
-
method that includes ammonium sulfate fraction, phenyl-Sepharose HR chromatographies and amminohexyl-Sepharose anion exchange
-
partial on DEAE-cellulose, two peaks of activity: peak I contains ro isoform and peak II contains subunits alpha and beta
-
two methods: the first involved purification of the His-tagged protein under denaturing conditions of 8M urea and the second involved separation of SDS-PAGE
recombinant MAT II purified by a method that includes Ni-agarose bead affinity capture. Alternative method includes Triton X-100 and 8 mM urea buffered extraction of inclusion body phase and dialysis
-
recombinant enzyme purified by a method that includes Ni2+-His binding resin, HiLoad Q-Sepharose and Sephadex-200 chromatography
-
two isoenzymes: I and II
-
partial
-
recombinant protein
2 forms: high-MW form and low-MW form
-
alpha isozyme from liver using immunoaffinity chromatography; beta isoenzyme from liver using several chromatographic steps
-
gamma isoenzyme from kidney
-
method that includes DEAE-Sephacel chromatography and phenyl Sepharose CL-4B chromatography
-
method that includes DEAE-Sepharose, phenyl-Sepharose and blue-Sepharose chromatographies and ultrafiltration
-
three isoforms: MAT-I, MAT-II and MAT-III, MAT-III to homogeneity
-
Ni2+-IDA agarose column chromatography
-
partial, two forms: I and II
-
recombinant protein
-
recombinant His-tagged enzyme from Escherichia coli strain XL-1 Blue by nickel affiniy chromatography
recombinant protein; recombinant protein
partial, S-adenosylmethionine synthetase B; two isoforms: A and B
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene SAMS1, a housekeeping gene, DNA and amino acid sequence determination and analysis, expression analysis and regulation, overview, expression of soluble His-tagged isozyme SAMS1 in Escherichia coli strain M15; gene SAMS2, a housekeeping gene, DNA and amino acid sequence determination and analysis, expression analysis and regulation, overview; gene SAMS3, a housekeeping gene, DNA and amino acid sequence determination and analysis, expression analysis and regulation, overview; gene SAMS4, a housekeeping gene, DNA and amino acid sequence determination and analysis, expression analysis and regulation, overview
expressed in Escherichia coli BL21 (DE3) cells
three isoenzymes expressed in Escherichia coli; three isoenzymes expressed in Escherichia coli; three isoenzymes expressed in Escherichia coli
expressed in Escherichia coli strain SG10039
-
gene MAT, DNA and amino acid sequence determination and analysis, expression analysis
gene metK, expression in Bacillus subtilis
-
expression in Escherichia coli
-
gene metK, expression in a metK deletion mutant Escherichia coli strain MOB1490
-
alpha subunit expressed in Escherichia coli NM522 strain
-
cloning and sequencing of the MAT 2A cDNA from lung epithelial cells reveals one silent nucleotide substitution compared to that expressed in Jurkat cells
expressed in Escherichia coli M15(Qiagen)
expressed in Hep-G2 cells, HuH-7 cells, and HCC cells
-
expressed in M15 bacteria
-
His-tagged recombinant MAT II alpha2 subunit expressed in COS-1 cells
-
expressed in Escherichia coli XL-1Blue strain
-
gene MAT-2, stable expression in Leishmania donovani promastigotes, phenotypic effects, overview
-
His6-tagged fusion protein expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)codon plus/pMJ1208-strain with a decahistidine tag on the N-terminus
-
expression in Escherichia coli
-
expressed in Escherichia coli strain BL21(DE3) RIL
expressed in Escherichia coli strain BL21(DE3) RIL
expressed in Escherichia coli strain BL21(DE3) RIL
expression in Escheriochia coli
expressed in Escherichia coli BL21(DE3)
-
gene metK, DNA and amino acid sequence determination and analysis, expression in and complementation of an Escherichia coli metK deletion strain
-
expressed in Pichia pastoris
-
expressed in Streptomyces actuosus
-
expression in Escherichia coli
-
gene SAM-s, DNA and amino acid sequence determination and analysis, a putative purine-rich ribosomal binding site is located 3 bp upstream of the GTG start codon, potential -35 and -10 consensus promoter sequences, expression of His-tagged enzyme in Escherichia coli strain XL-1 Blue, overexpression in Streptomyces avermitilis leads to 2fold increased synthesis of the antibiotic avermectin, overexpression in Streptomyces peucetius leads to 3.5fold increased synthesis of the antibiotic doxorubicin
chromosomal integration and expression in Saccharopolyspora erythraea strain E2 resulting in the overexpressing strain E1, subcloning in Escherichia coli strains ET12567 and DH5alpha
-
expressed in Pichia pastoris strain GS115
expression in Nicotiana tabacum
-
expression in Escherichia coli
subunit MAT2beta
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
S-adenosylmethionine synthase is one of the genes highly expressed under salt stress. Expression increases to 4.5fold after 2 h and to 5.8fold after 24 h of salt stress
-
transcripts for the isoform metK1-sp are repressed as Streptomyces cells enter the decline phase
transcripts for the isoform metK1-sp are induced as Streptomyces cells enter the decline phase
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D107C
-
enzyme activity similar to wild-type, attachment of methanethiosulfonate spin label to form D107R1, increase in Km-value, decrease in kcat value
D121N
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no basal enzymic activity, little activity in presence of S-adenosyl methionine
D166N
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reduced enzymic activity, little activation by S-adenosyl methionine
D19N
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no basal enzymic activity, little activity in presence of S-adenosyl methionine
D249N
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reduced enzymic activity, little activation by S-adenosyl methionine
D277N
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no enzymic activity
D282N
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reduced enzymic activity, little activation by S-adenosyl methionine
F241A
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no enzymic activity, but hydrolysis of triphosphate
H17A
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no basal enzymic activity, little activity in presence of S-adenosyl methionine
H17N
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no basal enzymic activity, little activity in presence of S-adenosyl methionine
K168A
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no enzymic activity
K256A
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no activation by S-adenosyl methionine
K276A
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no enzymic activity
K280A
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enhanced enzymic activity, little activation by S-adenosyl methionine
R255L
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no enzymic activity
W387F
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kinetic data
W387F
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
W387F/Y120W
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kinetic data
W387F/Y120W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y170W
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kinetic data
W387F/Y170W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y226W
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kinetic data
W387F/Y226W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y233W
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4.9fold increase in kcat value. Mutant shows three transitions in urea titration curve, contrary to two transitions of wild-type
W387F/Y233W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y255W
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fluorescence intensity reduced to 18% of wild-type
W387F/Y255W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y267W
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kinetic data
W387F/Y267W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y273W
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kinetic data
W387F/Y273W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y323W
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kinetic data
W387F/Y323W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a delayed first transition
W387F/Y344W
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kinetic data
W387F/Y344W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition
W387F/Y371W
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shows one transition in urea titration curve, contrary to two transitions of wild-type
W387F/Y371W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a delayed first transition
W387F/Y49W
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decrease in kcat value by 32%
W387F/Y49W
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition
W387F/Y72W
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kinetic data
W387F/Y72W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme and mutant enzyme W387F/Y72W in guanidinium chloride is a three-state process. Lower resistance to guanidinium chloride than the wild type enzyme
W387F/Y85W
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kinetic data
W387F/Y85W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
W387F
-
the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
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W387F/Y120W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme
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W387F/Y49W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition
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W387F/Y72W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme and mutant enzyme W387F/Y72W in guanidinium chloride is a three-state process. Lower resistance to guanidinium chloride than the wild type enzyme
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C35S
reduction in Vmax value
C61S
reduction in Vmax value
additional information
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a single mutant metK10 with one nucleotide substitution in the metK gene resulting in a 15fold decrease in SAM synthetase activity and a 4fold decrease in SAM concentration in vivo, the metK10 mutation specifically affects S-box gene expression, and the increase in expression under repressing conditions is dependent on the presence of a functional transcriptional antiterminator element, phenotype, overview
additional information
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mutational analysis and structural mapping of the the S(MK) box, conserved RNA motif in the 5'-untranslated region of the metK gene, overview
G105C
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enzyme activity similar to wild-type, attachment of methanethiosulfonate spin label to form G105R1, increase in Km-value
additional information
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mutants D107R1, D105R1, derived from mutants D107C, D105C, by addition of methanethiosulfonate spin label
additional information
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construction of a metK deletion mutant strain MOB1490 from wild-type strain BW25113, complementation by wild-type gene metK, as well as by genes metK from Rickettsia prowazekii and Rickettsia typhi, overview
additional information
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recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
W387F/Y85W
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the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride
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additional information
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expression of dihydrodipicolinate synthase or co-expression of cystathionine gamma-synthase and dihydrodipicolinate synthase from Arabidopsis thaliana in tobacco leaves and seeds results in enhanced methionine levels, overview
F251D
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inactive, but displays correct nuclear localization and matrix binding
additional information
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MAT1A knockout mice, spontaneous steatohepatitis develops by 8 months, hepatocellular carcinoma develops by 18 months
H145Y
spontaneous mutant, excretes a large amount of a red compound identified as coproporphyrin III. The mutant is able to grow under phototrophic conditions but has low levels of intracellular cysteine and glutathione and overexpresses the cysteine synthase CysK. The wild-type phenotype is restored when the gene metK encoding SAM synthetase is supplied in trans. The mutation is responsible for a 70% decrease in intracellular SAM content which probably affects the activities of numerous SAM-dependent enzymes such as coproporphyrinogen oxidase, uroporphyrinogen III methyltransferase, and molybdenum cofactor biosynthesis protein A
additional information
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mutations that affect the function of the metK gene products are a stop codon in the Madrid E strain and a 6-bp deletion in the Breinl strain, these typhus group genes, like the more degenerate spotted fever group orthologs, are in the process of gene degradation, overview
additional information
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
additional information
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improved production of erythromycin A by expression of MAT in Saccharopolyspora erythraea E1
additional information
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. The K18R mutation of Streptomyces spectabilis probably result in the increased activity of the best MAT. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
additional information
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overexpression in Nicotiana tabacum using Agrobacterium tumefaciens-mediated transformation results in active SAMS2 and accumulation of soluble polyamines
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding by a fourfold dilution refolding buffer up to a concentration of 2 M urea
-
in 50 mM Tris-HCl (pH 8.0), 10 mM MgSO4, and 10 mM dithiothreitol
in 50 mM Tris-HCl (pH 8.0), 10 mM MgSO4, and 10 mM dithiothreitol
in 50 mM Tris-HCl (pH 8.0), 10 mM MgSO4, and 10 mM dithiothreitol
dithiothreitol-refolding in the presence or absence of 250 mM CuSO4; dithiothreitol-refolding in the presence or absence of 250 mM CuSO4; dithiothreitol-refolding in the presence or absence of 250 mM CuSO4
refolding by direct dialysis or by dilution after treatment with urea under several conditions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
medicine
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patients with acoholic liver disease, decrease in hepatic enzyme activity due to decreased MAT1A expression and inactivation of MAT1A-encoded isoenzymes
medicine
-
S-adenosyl-L-methionine is applied to patients with alcoholic liver disease
medicine
-
animals fed ethanol intragastrically for 9 weeks switch hepatic MAT expression from MAT1A to MAT2A followed by decrease in S-adenosylmethionine levels, hypomethylation of c-myc, increase in c-myc expression and increased DNA strand break accumulation; MAT1A knockout mice, spontaneous steatohepatitis develops by 8 months, hepatocellular carcinoma develops by 18 months
synthesis
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain
synthesis
-
improved production of erythromycin A by expression of a heterologous gene encoding S-adenosylmethionine synthetase in Saccharopolyspora erythraea
synthesis
-
recombination of MAT genes from Escherichia coli, Saccharomyces cerevisiae, and Streptomyces spectabilis by DNA shuffling and transformation into Pichia pastoris. In the two best recombinant strains, the MAT activities are respectively 201% and 65% higher than the recombinant strains containing the starting MAT genes, and the SAM concentration increases by 103% and 65%, respectively. The K18R mutation of Streptomyces spectabilis probably result in the increased activity of the best MAT. A 6.14 g/l of SAM production is reached in a 500 l bioreactor with the best recombinant strain