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Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P54419

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Bacillus subtilis
UNIPROT: P54419 not found.
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Word Map
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  • 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: Bacillus subtilis
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-adenosylmethionine synthetase
-
SAM synthetase
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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
SAM synthase
-
-
SAM 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
-
-
-
?
ATP + D,L-methionine-(methyl-D3) + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
0.02 mM stimulates activity
Co2+
0.02 mM stimulates activity
K+
0.2 mM stimulates activity
Mg2+
required for activity
Ni2+
0.02 mM stimulates activity
Zn2+
0.02 mM stimulates activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.92
ATP
in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37°C
0.26
L-methionine
in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
gel filtration
45000
4 * 45000, dimer of dimer, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 45000, dimer of dimer, gel filtration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I105A/I317A
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the conversion of the natural substrate methionine is reduced in this mutant
I105V/I317A
-
the conversion of the natural substrate methionine is reduced in this mutant
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McDaniel, B.A.; Grundy, F.J.; Kurlekar, V.P.; Tomsic, J.; Henkin, T.M.
Identification of a mutation in the Bacillus subtilis S-adenosylmethionine synthetase gene that results in derepression of S-box gene expression
J. Bacteriol.
188
3674-3681
2006
Bacillus subtilis
Manually annotated by BRENDA team
Kamarthapu, V.; Rao, K.V.; Srinivas, P.N.; Reddy, G.B.; Reddy, V.D.
Structural and kinetic properties of Bacillus subtilis S-adenosylmethionine synthetase expressed in Escherichia coli
Biochim. Biophys. Acta
1784
1949-1958
2008
Bacillus subtilis (P54419), Bacillus subtilis
Manually annotated by BRENDA team
Dippe, M.; Brandt, W.; Rost, H.; Porzel, A.; Schmidt, J.; Wessjohann, L.A.
Rationally engineered variants of S-adenosylmethionine (SAM) synthase: reduced product inhibition and synthesis of artificial cofactor homologues
Chem. Commun. (Camb.)
51
3637-3640
2015
Bacillus subtilis, Bacillus subtilis ATCC 6051
Manually annotated by BRENDA team