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Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P19358

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Saccharomyces cerevisiae
UNIPROT: P19358 not found.
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Word Map
hide
  • 2.5.1.6
  • monolayers
  • self-assembled
  • gold
  • film
  • alkanethiols
  • photoelectron
  • infrared
  • fabric
  • electrode
  • electrochemical
  • tunnel
  • voltammetry
  • coverage
  • interfacial
  • ellipsometry
  • impedance
  • s-adenosylhomocysteine
  • thiolate
  • silicon
  • photoemission
  • electrochemistry
  • well-ordered
  • photovoltaic
  • wafer
  • large-area
  • transistor
  • transmethylation
  • semiconductor
  • nanoscopic
  • field-effect
  • close-packed
  • stamp
  • photolithography
  • wettabl
  • nanopatterns
  • polycrystalline
  • electroless
  • thin-film
  • chemisorption
  • drug development
  • lithography
  • microcontact
  • fermi
  • headgroups
  • wettability
  • synthesis
  • medicine
  • micropatterned
  • microbalance
  • silane
  • statin-associated
  • transsulfuration
  • ferrocene
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
sams, mat2a, methionine adenosyltransferase, mat1a, s-adenosylmethionine synthetase, adomet synthetase, sam synthetase, mat ii, matalpha2, s-adenosyl-l-methionine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP: L-methionine S-adenosyltransferase
-
S-adenosylmethionine synthetase
-
S-adenosylmethionine synthetase 2
-
S-adenosylmethionine-L-synthetase
-
adenosylmethionine synthetase
-
-
-
-
AdoMet synthetase
-
-
-
-
ATP-methionine adenosyltransferase
-
-
-
-
methionine adenosyltransferase
-
-
-
-
methionine S-adenosyltransferase
-
-
-
-
methionine-activating enzyme
-
-
-
-
S-adenosyl-L-methionine synthetase
-
-
-
-
S-adenosylmethionine synthase
-
-
-
-
S-adenosylmethionine synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-methionine S-adenosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9012-52-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
slight activation
Mg2+
-
up to 20% activation
Mn2+
-
slight activiation
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
causes complete inactivation of the enzyme
ATP
causes complete inactivation of the enzyme
Ba2+
70.70% residual activity at 5 mM
Br-
93.33% residual activity at 5 mM
Ca2+
86.36% residual activity at 5 mM
CH3COO-
92.25% residual activity at 5 mM
Cl-
85.27% residual activity at 5 mM
Cu2+
25.74% residual activity at 5 mM
F-
88.84% residual activity at 5 mM
Fe2+
59.22% residual activity at 5 mM
GSH
causes complete inactivation of the enzyme
I-
87.91% residual activity at 5 mM
K+
85.27% residual activity at 5 mM
Li+
81.40% residual activity at 5 mM
Mn2+
73.49% residual activity at 5 mM
Na+
80.16% residual activity at 5 mM
Zn2+
22.17% residual activity at 5 mM
1-aminocyclopentanecarboxylic acid
-
-
alpha,beta-methylene-adenosine tetraphosphate
-
-
alpha,beta-methylene-ATP
-
-
beta,gamma-methylene-ATP
-
-
DL-2-Amino-trans-4-hexenoic acid
-
-
L-2-Amino-4-hexynoic acid
-
-
S-Trifluoromethyl-L-homocysteine
-
-
Tetrapolyphosphate
-
-
tripolyphosphate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
sorbitol
53.26% increased yield of S-adenosyl-L-methionine at 1.2% sorbitol
additional information
no significant effect in the presence of n-dodecane
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.631
ATP
at pH 8.0 and 35°C
0.527
L-methionine
at pH 8.0 and 35°C
0.33
ATP
-
pH 8.0, 37°C
0.12
L-methionine
-
pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
Tetrapolyphosphate
-
-
0.05
tripolyphosphate
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23.83
after 3.71fold purification, at 35°C
6.42
crude extract, at 35°C
0.94
-
pH 8.0, 37°C
11
-
isoenzyme II
18.7
-
isoenzyme I
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
more than 60% of maximum activity within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
50% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the product S-adenosyl-L-methionine plays important roles in trans-methylation, transsulfuration, and polyamine synthesis in all living cells
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
forms I and II, gel filtration
43600
-
x * 43600, ESI-MS
55000
-
1 * 55000 + 1 * 60000, SDS-PAGE
60000
-
1 * 55000 + 1 * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 43600, ESI-MS
dimer
-
1 * 55000 + 1 * 60000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
the activity of the enzyme is decreased above pH 9.0 and is inactive at pH below 7.5
685773
5
-
easily inactivated below
706910
7 - 9
-
-
706910
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
enzyme activity is significantly reduced at temperatures below 30°C or above 40°C
45
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the Ni2+-IDA agarose-immobilized synthetase exhibits 40.4% of the free enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-IDA agarose column chromatography
partial, two forms: I and II
-
recombinant protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a multiple-copy integrative plasmid pYMIKP-SAM2 is introduced into the chromosome of wild-type Saccharomyces cerevisiae strain ZJU001 to construct the recombined strain R1-ZJU001
expressed in Pichia pastoris
expressed in Streptomyces actuosus
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the product S-adenosyl-L-methionine is an effective cure for liver disease, depressive syndromes, and osteoarthritis. A multiple-copy integrative plasmid pYMIKP-SAM2 is introduced into the chromosome of wild-type Saccharomyces cerevisiae strain ZJU001 to construct the recombined strain R1-ZJU001. The recombinant yeast exhibits higher enzymatic activity of methionine adenosyltransferase and improved S-adenosyl-L-methionine biosynthesis. With a three-phase fed-batch strategy in 15-liter bench-top fermentor, 8.81 g/l S-adenosyl-L-methionine is achieved after 52 h cultivation of R1-ZJU001, about 27.1 % increase over its parent strain ZJU001, whereas the S-adenosyl-L-methionine content is also improved from 64.6 mg/g dry cell weight to 91.0 mg/g dry cell weight
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chou, T.C.; Talalay, P.
Inhibition of ATP: L-methionine S-adenosyltransferase of bakers yeast by structural analogues of ATP
Biochim. Biophys. Acta
321
467-474
1973
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chou, T.C.; Talalay, P.
The mechanism of S-adenosyl-L-methionine synthesis by purified preparations of bakers yeast
Biochemistry
11
1065-1073
1972
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chiang, P.K.; Cantoni, G.L.
Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of bakers yeast and its separation into two forms
J. Biol. Chem.
252
4506-4513
1977
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zhang, X.; Fen, M.; Shi, X.; Bai, L.; Zhou, P.
Overexpression of yeast S-adenosylmethionine synthetase metK in Streptomyces actuosus leads to increased production of nosiheptide
Appl. Microbiol. Biotechnol.
78
991-995
2008
Saccharomyces cerevisiae (P19358), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Luo, Y.; Yuan, Z.; Luo, G.; Zhao, F.
Expression of secreted His-tagged S-adenosylmethionine synthetase in the methylotrophic yeast Pichia pastoris and its characterization, one-step purification, and immobilization
Biotechnol. Prog.
24
214-220
2008
Saccharomyces cerevisiae (P19358), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zhang, J.G.; Wang, X.D.; Zhang, J.N.; Wei, D.Z.
Oxygen vectors used for S-adenosylmethionine production in recombinant Pichia pastoris with sorbitol as supplemental carbon source
J. Biosci. Bioeng.
105
335-340
2008
Saccharomyces cerevisiae (P19358)
Manually annotated by BRENDA team
Hu, H.; Qian, J.; Chu, J.; Wang, Y.; Zhuang, Y.; Zhang, S.
DNA shuffling of methionine adenosyltransferase gene leads to improved S-adenosyl-L-methionine production in Pichia pastoris
J. Biotechnol.
141
97-103
2009
Streptomyces spectabilis, Escherichia coli (P0A817), Escherichia coli, Saccharomyces cerevisiae (P19358)
Manually annotated by BRENDA team
Zhou, J.; Chu, J.; Wang, Y.; Zhang, S.; Zhuang, Y.; Yuan, Z.
Purification and properties of Saccharomyces cerevisiae S-adenosylmethionine synthetase expressed in recombinant Pichia pastoris
World J. Microbiol. Biotechnol.
24
789-796
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zhao, W.; Shi, F.; Hang, B.; Huang, L.; Cai, J.; Xu, Z.
The improvement of SAM accumulation by integrating the endogenous methionine adenosyltransferase gene SAM2 in genome of the industrial Saccharomyces cerevisiae strain
Appl. Biochem. Biotechnol.
178
1263-1272
2016
Saccharomyces cerevisiae (P19358), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741 (P19358)
Manually annotated by BRENDA team