Any feedback?
Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A817
for references in articles please use BRENDA:EC2.5.1.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.5.1.6 methionine adenosyltransferaseSpecify your search results
Word Map
- 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: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
-
-
-
methionine adenosyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
mechanism of inhibiton by product analogues and implications for reaction
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
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
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'
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
adenosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:L-methionine S-adenosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9012-52-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
tripolyphosphate + H2O
diphosphate + phosphate
-
tripolyphosphatase activity
-
?
additional information
?
-
S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants
-
-
?
additional information
?
-
-
S-adenosylmethionine synthesis and tripolyphosphatase activity messured for six aspartate-mutants
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Co2+
K+
Mg2+
Mn2+
additional information
-
divalent cations are required for tripolyphosphatase activity
Co2+
-
for maximal activation the cation concentration must be at least equal to ATP concentration
Mg2+
-
cation concentration must be at least equal to ATP concentration for maximal activity
Mn2+
-
for maximal activation the cation concentration must be at least equal to ATP concentration
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
S-adenosyl-L-methionine
-
product inhibition. Compared with the wild-type MAT, as little as 200 mM sodium p-toluenesulfonate is required to completely overcome the product inhibition of I303V mutant enzyme on a 30 mM scale incubation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.03 - 0.038
L-methionine
-
one kinetic form of alpha subunit in the presence of beta subunit
0.065 - 0.08
L-methionine
-
alpha subunit at low L-methionine concentrations
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000000367
S-adenosylmethionine
RLL mutant, S-adenosylmethionine synthesis
0.00000045
S-adenosylmethionine
G6 mutant, S-adenosylmethionine synthesis
0.000000667
S-adenosylmethionine
G8 mutant, S-adenosylmethionine synthesis
0.00000217
S-adenosylmethionine
G5 mutant, S-adenosylmethionine synthesis
0.000012
S-adenosylmethionine
G7 mutant, S-adenosylmethionine synthesis
0.000417
S-adenosylmethionine
wild-type, S-adenosylmethionine synthesis
0.00000122
tripolyphosphate
RLL and G7 mutants, tripolyphosphatase activity
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
about 20% activity at 20°C, about 30% activity at 30°C, about 80% activity at 35°C, about 90% activity at 40°C, 100% at 45°C, about 850% activity at 50°C, about 45% activity at 60°C, and no activity at 70°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
43000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
tetramer
two subunits form a spherical dimer and pairs of these dimers form a tetrameric enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylation
12 lysine residues of the protein are acetylated. Acetylation lead to a decrease in its enzymatic activity, which could be reversed by CobB deacetylation. Lysine acetylation regulates the activity of the enzyme
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
quantum mechanical/molecular mechanical calculations, exploiting structures of the active crystalline enzyme, based on PDB files 1P7L and 1RG9
method of vapor diffusion, hexagonal bipiramid crystals in the presence of Mg2+ and diphosphate
-
PROTEIN VARIANTS
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
G105C
enzyme activity similar to wild-type, attachment of methanethiosulfonate spin label to form G105R1, increase in Km-value
I303V/I65V/L186V
product inhibition of the enzyme is reduced via semi-rational modification. The mutant enzyme shows a 42fold increase in Ki(ATP) and a 2.08fold increase in specific activity when compared to wild-type enzyme. Its Ki(ATP) is 0.42 mM and specific acitivity is 3.78 U/mg. Increased Ki(ATP) means reduced product inhibition which enhances accumulation of S-adenosyl-L-methionine. The S-adenosyl-L-methionine produced by the variant could reach to 3.27 mM while S-adenosyl-L-methionine produced by wild-type enzyme is 1.62 mM in the presence of 10 mM substrates
I303V/I65V/L186V/N104K
product inhibition of the enzyme is reduced via semi-rational modification. The mutant enzyme shows a 3.3fold increase in specific activity when compared to wild-type enzyme. Specific acitivity of the mutant enzyme is 6.02 U/mg. Increased Ki(ATP) means reduced product inhibition which enhances accumulation of S-adenosyl-L-methionine. The S-adenosyl-L-methionine produced by the variant could reach to 2.68 mM while S-adenosyl-L-methionine produced by wild-type enzyme is 1.62 mM in the presence of 10 mM substrates
I303V
-
the Km-values for both substrates are slightly less than those of the wild-type enzyme. The variant is successfully produced at a high level (about 800 mg/l) with approximately four-fold higher specific activity than the wild-type enzyme. The recombinant mutant enzyme is covalently immobilized onto the amino resin and epoxy resin in order to obtain a robust biocatalyst to be used in industrial bioreactors. The immobilized preparation using amino resin exhibits the highest activity coupling yield (about 84%), compared with approximately 3% for epoxy resin. The immobilized mutant enzyme is more stable than the soluble enzyme under the reactive conditions, with a half-life of 229.5 h at 37 °C. The Km(ATP) value (0.18 mM) of the immobilized mutant enzyme is about two-fold lower than that of the soluble enzyme. The immobilized enzyme shows high operational stability during 10 consecutive 8 h batches, with the substrate adenosine triphosphate conversion rate above 95% on the 50 mM scale. Compared with the wild-type enzyme, as little as 200 mM sodium p-toluenesulfonate is required to completely overcome the product inhibition by S-adenosyl-L-methionine of I303V mutant enzyme on a 30 mM scale incubation
additional information
additional information
mutants D107R1, D105R1, derived from mutants D107C, D105C, by addition of methanethiosulfonate spin label
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
-
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
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
the enzyme activity remains stable after 2 h preincubation at 20-40°C in Tris-HCl (pH 8.9)
37
-
30% loss of activity after 12 h, complete loss of activity after 36-48 h, soluble enzyme. 63% of the initial enzyme activity of immobilized MAT was remained after 168 h incubation. Comparing the t1/2 values at 37 °C, the immobilized enzyme is almost 25fold more stable than the free enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the immobilized enzyme shows high operational stability during 10 consecutive 8 h batches
-
thermal stability of the immobilized enzyme is much higher than that of the soluble enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
ammonium sulfate precipitation and phenyl Sepharose 6 column chromatography
-
His6-tagged wild-type and I303V mutant proteins are purified in a single chromatography step usinf a HiTrap chelating nickel column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene metK, expression in a metK deletion mutant Escherichia coli strain MOB1490
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Markham, G.D.; Hafner, E.W.; White Tabor, C.; Tabor, H.
S-adenosylmethionine synthetase (methionine adenosyltransferase) (Escherichia coli)
Methods Enzymol.
94
219-222
1983
Escherichia coli
Gilliland, G.L.; Markham, G.D.; Davies, D.R.
S-adenosylmethionine synthetase from Escherichia coli. Crystallization and preliminary X-ray diffraction studies
J. Biol. Chem.
258
6963-6964
1983
Escherichia coli
Markham, G.D.; Hafner, E.W.; White Tabor, C.; Tabor, H.
S-Adenosylmethionine synthetase from Escherichia coli
J. Biol. Chem.
255
9082-9092
1980
Escherichia coli
Takusagawa, F.; Kamitori, S.; Markham, G.D.
Structure and function of S-adenosylmethionine synthetase: Crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 2.8.ANG. resolution
Biochemistry
35
2586-2596
1996
Escherichia coli (P0A817), Escherichia coli
Taylor, J.C.; Markham, G.D.
The bifunctional active site of S-adenosylmethionine synthetase. Roles of the active site aspartates
J. Biol. Chem.
274
32909-32914
1999
Escherichia coli (P0A817), Escherichia coli, Escherichia coli XL1-Blue (P0A817)
LeGros, H.L., Jr.; Halim, A.B.; Geller, A.M.; Kotb, M.
Cloning, expression, and functional characterization of the b regulatory subunit of human methionine adenosyltransferase (MAT II)
J. Biol. Chem.
275
2359-2366
2000
Escherichia coli, Homo sapiens, Homo sapiens (Q9NZL9)
Corrales, F.J.; Perez-Mato, I.; Sanchez Del Pino, M.M.; Ruiz, F.; Castro, C.; Garcia-Trevijano, E.R.; Latasa, U.; Martinez-Chantar, M.L.; Martinez-Cruz, A.; Avila, M.A.; Mato, J.M.
Regulation of mammalian liver methionine adenosyltransferase
J. Nutr.
132
2377S-2381S
2002
Escherichia coli, Homo sapiens, Rattus norvegicus
Taylor, J.C.; Takusagawa, F.; Markham, G.D.
The active site loop of S-adenosylmethionine synthetase modulates catalytic efficiency
Biochemistry
41
9358-9369
2002
Escherichia coli (P0A817), Escherichia coli, Escherichia coli XL1-Blue (P0A817)
Taylor, J.C.; Markham, G.D.
Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by site-directed spin labeling
Arch. Biochem. Biophys.
415
164-171
2003
Escherichia coli (P0A817)
Komoto, J.; Yamada, T.; Takata, Y.; Markham, G.D.; Takusagawa, F.
Crystal structure of the S-adenosylmethionine synthetase ternary complex: a novel catalytic mechanism of S-adenosylmethionine synthesis from ATP and Met
Biochemistry
43
1821-1831
2004
Escherichia coli (P0A817), Escherichia coli
Markham, G.D.; Reczkowski, R.S.
Structural studies of inhibition of S-adenosylmethionine synthetase by slow, tight-binding intermediate and product analogues
Biochemistry
43
3415-3425
2004
Escherichia coli (P0A817)
Driskell, L.O.; Tucker, A.M.; Winkler, H.H.; Wood, D.O.
Rickettsial metK-encoded methionine adenosyltransferase expression in an Escherichia coli metK deletion strain
J. Bacteriol.
187
5719-5722
2005
Escherichia coli, Rickettsia prowazekii, Rickettsia typhi
Markham, G.D.; Takusagawa, F.; Dijulio, A.M.; Bock, C.W.
An investigation of the catalytic mechanism of S-adenosylmethionine synthetase by QM/MM calculations
Arch. Biochem. Biophys.
492
82-92
2009
Escherichia coli (P0A817)
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)
Taylor, J.C.; Bock, C.W.; Takusagawa, F.; Markham, G.D.
Discovery of novel types of inhibitors of S-adenosylmethionine synthesis by virtual screening
J. Med. Chem.
52
5967-5973
2009
Escherichia coli (P0A817)
Yao, G.; Qin, X.; Chu, J.; Wu, X.; Qian, J.
Expression, purification, and characterization of a recombinant methionine adenosyltransferase pDS16 in Pichia pastoris
Appl. Biochem. Biotechnol.
172
1241-1253
2014
Escherichia coli
Sun, M.; Guo, H.; Lu, G.; Gu, J.; Wang, X.; Zhang, X.E.; Deng, J.
Lysine acetylation regulates the activity of Escherichia coli S-adenosylmethionine synthase
Acta Biochim. Biophys. Sin. (Shanghai)
48
723-731
2016
Escherichia coli (P0A817), Escherichia coli
Niu, W.; Cao, S.; Yang, M.; Xu, L.
Enzymatic synthesis of S-adenosylmethionine using immobilized methionine adenosyltransferase variants on the 50-mM scale
Catalysts
7
238
2017
Escherichia coli, Escherichia coli BL21 (DE3)
-
Wang, X.; Jiang, Y.; Wu, M.; Zhu, L.; Yang, L.; Lin, J.
Semi-rationally engineered variants of S-adenosylmethionine synthetase from Escherichia coli with reduced product inhibition and improved catalytic activity
Enzyme Microb. Technol.
129
109355
2019
Escherichia coli (P0A817), Escherichia coli, Escherichia coli K12 (P0A817)
EXTERNAL LINKS (specific for EC-Number 2.5.1.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
