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Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Atriplex nummularia and UniProt Accession Q6F3F0

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This record set is specific for:
Atriplex nummularia
UNIPROT: Q6F3F0 not found.
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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: Atriplex nummularia
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
S-adenosyl-L-methionine synthetase
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SAM synthetase
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adenosylmethionine synthetase
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-
-
-
AdoMet synthetase
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-
-
-
ATP-methionine adenosyltransferase
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-
-
-
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
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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
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
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
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
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.109
purified recombinant His-tagged isozyme SAMS1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme SAMS3; a halophyte, isozyme SAMS3
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
METK3_ATRNU
396
0
43139
Swiss-Prot
other Location (Reliability: 2)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozyme SAMS1 from Escherichia coli strain M15
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SAMS3, a housekeeping gene, DNA and amino acid sequence determination and analysis, expression analysis and regulation, overview
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 SAMS4, a housekeeping gene, DNA and amino acid sequence determination and analysis, expression analysis and regulation, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tabuchi, T.; Kawaguchi, Y.; Azuma, T.; Nanmori, T.; Yasuda, T.
Similar regulation patterns of choline monooxygenase, phosphoethanolamine N-methyltransferase and S-adenosyl-L-methionine synthetase in leaves of the halophyte Atriplex nummularia L
Plant Cell Physiol.
46
505-513
2005
Atriplex nummularia (Q6F3F0), Atriplex nummularia (Q6F3F1), Atriplex nummularia (Q6F3F3), Atriplex nummularia (Q7XZR1), Atriplex nummularia
Manually annotated by BRENDA team