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Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Homo sapiens and UniProt Accession P31153

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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: Homo sapiens
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
MAT IIalpha
-
MAT2A
isoform
methionine adenosyl transferase 2A
-
methionine adenosyltransferase
-
methionine adenosyltransferase II
-
methionine adenosyltransferase II-alpha
-
methionine adenosyltransferase IIalpha
-
S-adenosylmethionine synthetase
-
adenosylmethionine synthetase
-
-
-
-
AdoMet synthetase
-
-
-
-
ATP-methionine adenosyltransferase
-
-
-
-
MAT1A
MAT2A
MAT2beta
-
regulatory subunit
MATalpha1
-
MATalpha2
catalytic subunit
methionine adenosyltransferase
methionine adenosyltransferase 2A
-
-
methionine adenosyltransferase 2beta
-
-
methionine adenosyltransferase alpha1
-
methionine S-adenosyltransferase
-
-
-
-
methionine-activating enzyme
-
-
-
-
S-adenosyl-L-methionine synthetase
-
-
-
-
S-adenosylmethionine synthase
-
-
-
-
S-adenosylmethionine synthetase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
-
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 + (3S)-3-amino-5-(methylthio)pentan-2-ol + H2O
phosphate + diphosphate + ?
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
ATP + S-(-)-methioninol + H2O
?
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-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
-
tripolyphosphatase activity
-
?
additional information
?
-
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
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cycloleucine
1-aminocyclopentane-1-carboxylic acid, specific MAT inhibitor
ethanol
25 mM ethanol substantially decreases the enzymatic activity of MAT II
Dimethylsulfoxide
-
-
diphosphate
-
-
Fumarylacetoacetate
-
reduces MAT I/III activity
hydrogen peroxide
-
reduces MAT I/III activity
L-methionine
-
-
methylthioadenosine
-
lowers expression of MAT2A and MAT2beta
p-chloromercuribenzoate
phosphate
-
-
S-adenosyl-L-methionine
-
feedback inhibition of isozyme MAT II
S-adenosylmethionine
tripolyphosphate
-
competitive with ATP and non competitive with L-methionine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Epidermal growth factor
-
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
insulin-like growth factor 1
-
100 ng/ml upregulates MAT2A (but not MAT2beta) expression
-
leptin
-
Tumor necrosis factor alpha
-
induces expression of variant 1 (but not variant 2) MAT2beta
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 0.14
L-methionine
0.39 - 2.4
S-(-)-methioninol
0.031
ATP
-
-
0.0061 - 3.3
L-methionine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.43
L-methionine
0.055 - 0.183
S-(-)-methioninol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.167 - 3.07
L-methionine
0.076 - 0.68
S-(-)-methioninol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0002
-
activity Peak II, adult erythrocytes
12.2
-
-
216
-
pH 7.0, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lung epithelial isoform of MAT 2A
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
T helper CD4+ lymphocyte
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
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
-
mainly MAT2beta variant 2
Manually annotated by BRENDA team
-
leukemia promyelotic cells
Manually annotated by BRENDA team
-
MAT2beta variant 1 and 2
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
Manually annotated by BRENDA team
-
mainly MAT2beta variant 2
Manually annotated by BRENDA team
-
mainly MAT2beta variant 1
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
methionine adenosyltransferase IIalpha (MAT IIalpha) is a key enzyme in methionine metabolism and is associated with uncontrolled cell proliferation in cancer
physiological function
methionine adenosyltransferase IIalpha (MAT IIalpha) is a key enzyme in methionine metabolism and is associated with uncontrolled cell proliferation in cancer
malfunction
knocking down MAT1A or overexpressing MafG or c-Maf enhances cholangiocarcinoma growth and invasion in vivo
metabolism
the enzyme is involved in S-adenosylmethionine synthesis in liver. MATalpha1 interacts mainly with Mnt in normal liver but this switches to c-Maf, MafG and c-Myc in cholestatic livers and cholangiocarcinoma. Knocking down MAT1A or overexpressing MafG or c-Maf enhances cholangiocarcinoma growth and invasion in vivo
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
METK2_HUMAN
395
0
43661
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
185000
-
equilibrium sedimentation studies
32500
-
beta subunit, gel filtration
38000 - 39000
MAT II beta subunit, gel filtration
51000
-
expression of the alpha subunit in E. coli, gel filtration
53000
60000
-
isoenzyme ro, Peak I, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
dimer
homodimer
x-ray crystallography
tetramer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using
in complex with S-adenosyl-L-methionine, L-methionine, and 4-nitrophenyl phosphate, vapor diffusion method, using 0.1 M HEPES pH 7.5 and 30% (w/v) PEG 600
sitting drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E70S
the mutant enzyme lacks appreciable activity in the presence of non-native methionine surrogates (3.2% S-(-)-methioninol, 240 min versus 25% L-Met, 20 min)
K289F
the mutant enzyme lacks selectivity (33% (3S)-3-amino-5-(methylthio)pentan-2-ol versus 30% L-Met, 240 min)
K289L
160fold inversion of the enzyme (hMAT2A) selectivity index for a non-native methionine analogue over the native substrate L-methionine. Structure elucidation of K289L reveales the mutant to be folded normally with minor observed repacking within the modified substrate pocket. It is an example of exchanging L-Met terminal carboxylate/amine recognition elements within the hMAT2A active-site to enable non-native bioorthgonal substrate utilization
K289S
mutant displays selectivity toward (3S)-3-amino-5-(methylthio)pentan-2-ol (38%, 240 min) over L-Met (14%, 240 min)
K289T
mutant displays selectivity toward (3S)-3-amino-5-(methylthio)pentan-2-ol (14%, 240 min) over L-Met (2.5%, 240 min)
Q113D
mutant displays selectivity toward (3S)-3-amino-5-(methylthio)pentan-2-ol (39%, 240 min) over L-Met (13%, 240 min)
A55D
the mutation reduces the enzyme activity by more than 50%
D258G
the mutation reduces the enzyme activity by more than 50%
I322M
the mutation reduces the enzyme activity by more than 50%
R264H
the mutation almost completely abolishes enzyme activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
stable for several hours, if protein concentration is above 0.1 mg/ml and ionic strength is at least 50 mM
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Cullin 3 (CUL3) targets methionine adenosyltransferase IIa (MAT IIalpha) and promotes its proteasomal degradation through the ubiquitylation-mediated pathway
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, less than 10% loss of activity after 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, HiTrap HP-Q column chromatography, and Superdex 200 gel filtration
Ni-NTA column chromatography, HiTrap HP-Q column chromatography, and Superdex 200 gel filtration
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 BL21(DE3) cells
alpha subunit expressed in Escherichia coli NM522 strain
-
expressed in Escherichia coli BL21(DE3) 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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MAT1A expression falls in hepatocytes and bile duct epithelial cells during chronic cholestasis and in human cholangiocarcinoma
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tallan, H.H.; Cohen, P.A.
Methionine adenosyltransferase: kinetic properties of human and rat liver enzymes
Biochem. Med.
16
234-250
1976
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kotb, M.; Kredich, N.M.
S-Adenosylmethionine synthetase from human lymphocytes. Purification and characterization
J. Biol. Chem.
260
3923-3930
1985
Homo sapiens
Manually annotated by BRENDA team
Langkamp-Henken, B.; Geller, A.M.; LeGros, H.L., Jr.; Price, J.O.; De la Rosa, J.; Kotb, M.
Characterization of distinct forms of methionine adenosyltransferase in nucleated, and mature human erythrocytes and erythroleukemic cells
Biochim. Biophys. Acta
1201
397-404
1994
Homo sapiens
Manually annotated by BRENDA team
De La Rosa, J.; Ostrowski, J.; Hryniewicz, M.M.; Kredich, N.M.; Kotb, M.; LeGros, H.L., Jr.; Valentine, M.; Geller, A.M.
Chromosomal localization and catalytic properties of the recombinant alpha subunit of human lymphocyte methionine adenosyltransferase
J. Biol. Chem.
270
21860-21868
1995
Homo sapiens
Manually annotated by BRENDA team
Halim, A.B.; LeGros, L.; Geller, A.; Kotb, M.
Expression and functional interaction of the catalytic and regulatory subunits of human methionine adenosyltransferase in mammalian cells
J. Biol. Chem.
274
29720-29725
1999
Homo sapiens
Manually annotated by BRENDA team
Chamberlin, M.E.; Ubagai, T.; Pao, V.Y.; Pearlstein, R.A.; Yang Chou, J.
Structural requirements for catalysis and dimerization of human methionine adenosyltransferase I/III
Arch. Biochem. Biophys.
373
56-62
2000
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lu, S.C.; Mato, J.M.
Role of methionine adenosyltransferase and S-adenosylmethionine in alcohol-associated liver cancer
Alcohol
35
227-234
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wang, S.H.; Kuo, S.C.; Chen, S.C.
High-performance liquid chromatography determination of methionine adenosyltransferase activity using catechol-O-methyltransferase-coupled fluorometric detection
Anal. Biochem.
319
13-20
2003
Homo sapiens
Manually annotated by BRENDA team
Panayiotidis, M.I.; Stabler, S.P.; Ahmad, A.; Pappa, A.; Legros, L.H.; Hernandez-Saavedra, D.; Schneider, B.K.; Allen, R.H.; Vasiliou, V.; McCord, J.M.; Kotb, M.; White, C.W.
Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia
Free Radic. Biol. Med.
40
348-358
2006
Homo sapiens (P31153), Homo sapiens
Manually annotated by BRENDA team
Lu, S.C.; Martinez-Chantar, M.L.; Mato, J.M.
Methionine adenosyltransferase and S-adenosylmethionine in alcoholic liver disease
J. Gastroenterol. Hepatol.
21
S61-S64
2006
Homo sapiens
-
Manually annotated by BRENDA team
Hote, P.T.; Sahoo, R.; Jani, T.S.; Ghare, S.S.; Chen, T.; Joshi-Barve, S.; McClain, C.J.; Barve, S.S.
Ethanol inhibits methionine adenosyltransferase II activity and S-adenosylmethionine biosynthesis and enhances caspase-3-dependent cell death in T lymphocytes: relevance to alcohol-induced immunosuppression
J. Nutr. Biochem.
19
384-391
2007
Homo sapiens (P31153)
Manually annotated by BRENDA team
Chen, H.; Xia, M.; Lin, M.; Yang, H.; Kuhlenkamp, J.; Li, T.; Sodir, N.M.; Chen, Y.H.; Josef-Lenz, H.; Laird, P.W.; Clarke, S.; Mato, J.M.; Lu, S.C.
Role of methionine adenosyltransferase 2A and S-adenosylmethionine in mitogen-induced growth of human colon cancer cells
Gastroenterology
133
207-218
2007
Homo sapiens, Mus musculus (Q3TH56)
Manually annotated by BRENDA team
Yang, H.; Ara, A.I.; Magilnick, N.; Xia, M.; Ramani, K.; Chen, H.; Lee, T.D.; Mato, J.M.; Lu, S.C.
Expression pattern, regulation, and functions of methionine adenosyltransferase 2beta splicing variants in hepatoma cells
Gastroenterology
134
281-291
2008
Homo sapiens
Manually annotated by BRENDA team
Ramani, K.; Yang, H.; Xia, M.; Ara, A.I.; Mato, J.M.; Lu, S.C.
Leptins mitogenic effect in human liver cancer cells requires induction of both methionine adenosyltransferase 2A and 2beta
Hepatology
47
521-531
2008
Homo sapiens
Manually annotated by BRENDA team
Vazquez-Chantada, M.; Ariz, U.; Varela-Rey, M.; Embade, N.; Martinez-Lopez, N.; Fernandez-Ramos, D.; Gomez-Santos, L.; Lamas, S.; Lu, S.C.; Martinez-Chantar, M.L.; Mato, J.M.
Evidence for LKB1/AMP-activated protein kinase/endothelial nitric oxide synthase cascade regulated by hepatocyte growth factor, S-adenosylmethionine, and nitric oxide in hepatocyte proliferation
Hepatology
49
608-617
2009
Homo sapiens
Manually annotated by BRENDA team
Ramani, K.; Yang, H.; Kuhlenkamp, J.; Tomasi, L.; Tsukamoto, H.; Mato, J.M.; Lu, S.C.
Changes in the expression of methionine adenosyltransferase genes and S-adenosylmethionine homeostasis during hepatic stellate cell activation
Hepatology
51
986-995
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Shafqat, N.; Muniz, J.R.; Pilka, E.S.; Papagrigoriou, E.; von Delft, F.; Oppermann, U.; Yue, W.W.
Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits
Biochem. J.
452
27-36
2013
Homo sapiens (P31153), Homo sapiens (Q00266), Homo sapiens
Manually annotated by BRENDA team
Murray, B.; Antonyuk, S.V.; Marina, A.; Lu, S.C.; Mato, J.M.; Hasnain, S.S.; Rojas, A.L.
Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes
Proc. Natl. Acad. Sci. USA
113
2104-2109
2016
Homo sapiens (Q9NZL9), Homo sapiens
Manually annotated by BRENDA team
Huber, T.D.; Clinger, J.A.; Liu, Y.; Xu, W.; Miller, M.D.; Phillips, G.N.; Thorson, J.S.
Methionine adenosyltransferase engineering to enable bioorthogonal platforms for AdoMet-utilizing enzymes
ACS Chem. Biol.
15
695-705
2020
Homo sapiens (P31153), Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Zhu, Z.H.; Yang, H.B.; Zhang, Y.; Zhao, X.N.; Zhang, M.; Liu, Y.B.; Xu, Y.Y.; Lei, Q.Y.
Cullin 3 targets methionine adenosyltransferase IIalpha for ubiquitylation-mediated degradation and regulates colorectal cancer cell proliferation
FEBS J.
283
2390-2402
2016
Homo sapiens (P31153), Homo sapiens
Manually annotated by BRENDA team
Yang, H.; Liu, T.; Wang, J.; Li, T.W.; Fan, W.; Peng, H.; Krishnan, A.; Gores, G.J.; Mato, J.M.; Lu, S.C.
Deregulated methionine adenosyltransferase alpha1, c-Myc, and Maf proteins together promote cholangiocarcinoma growth in mice and humans
Hepatology
64
439-455
2016
Homo sapiens (Q00266), Homo sapiens, Mus musculus (Q91X83), Mus musculus
Manually annotated by BRENDA team