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2.5.1.6: methionine adenosyltransferase

This is an abbreviated version!
For detailed information about methionine adenosyltransferase, go to the full flat file.

Word Map on EC 2.5.1.6

Reaction

ATP
+
L-methionine
 +
H2O
=
phosphate
 +
diphosphate
 +
S-adenosyl-L-methionine

Synonyms

(Met) adenosyltransferase 4, adenosylmethionine synthase, adenosylmethionine synthetase, AdoMet synthase, AdoMet synthease, AdoMet synthetase, AdoMetS, ATP-methionine adenosyltransferase, ATP: L-methionine S-adenosyltransferase, EC 2.4.2.13, MAT, MAT I, MAT II, MAT IIalpha, MAT III, MAT1A, MAT2, MAT2A, MAT2beta, MAT3, MAT4, MATalpha1, MATalpha2, methionine adenosyl transferase 2A, methionine adenosyltransferase, methionine adenosyltransferase 2A, methionine adenosyltransferase 2beta, methionine adenosyltransferase 4, methionine adenosyltransferase alpha1, methionine adenosyltransferase II, methionine adenosyltransferase II-alpha, methionine adenosyltransferase IIalpha, methionine S-adenosyltransferase, methionine-activating enzyme, MetK, Mj-MAT, MJ1208, pDS16, PF1866, PfMAT, S-adenosyl-L-methionine synthetase, S-adenosyl-Lmethionine synthetase, S-adenosyl-Met synthetase 3, S-adenosylmethionine synthase, S-adenosylmethionine synthetase, S-adenosylmethionine synthetase 1, S-adenosylmethionine synthetase 2, S-adenosylmethionine synthetase 3, S-adenosylmethionine synthetase A, S-adenosylmethionine synthetase B, S-adenosylmethionine-L-synthetase, SAM synthase, SAM synthetase, SAM-s, Sam1, SAM2, SAMS, SAMS1, SAMS2, SMAT, SSO0199

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.6 methionine adenosyltransferase

Purification

Purification on EC 2.5.1.6 - methionine adenosyltransferase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 forms: high-MW form and low-MW form
-
alpha isozyme from liver using immunoaffinity chromatography
-
ammonium sulfate precipitation and phenyl Sepharose 6 column chromatography
-
beta isoenzyme from liver using several chromatographic steps
-
gamma isoenzyme from kidney
-
His6-tagged wild-type and I303V mutant proteins are purified in a single chromatography step usinf a HiTrap chelating nickel column
-
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
method that includes DEAE-Sephacel chromatography and phenyl Sepharose CL-4B chromatography
-
method that includes DEAE-Sepharose, phenyl-Sepharose and blue-Sepharose chromatographies and ultrafiltration
-
Ni-IMAC column chromatography and Source 30Q column chromatography
-
Ni-NTA column chromatography
Ni-NTA column chromatography, and gel filtration
Ni-NTA column chromatography, and Superdex-200 gel filtration
Ni-NTA column chromatography, HiTrap HP-Q column chromatography, and Superdex 200 gel filtration
Ni2+-IDA agarose column chromatography
nickel affinity column chromatography
partial
partial on DEAE-cellulose, two peaks of activity: peak I contains ro isoform and peak II contains subunits alpha and beta
-
partial, S-adenosylmethionine synthetase B
-
partial, two forms: I and II
-
recombinant enzyme purified by a method that includes Ni2+-His binding resin, HiLoad Q-Sepharose and Sephadex-200 chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain XL-1 Blue by nickel affiniy chromatography
recombinant His-tagged isozyme SAMS1 from Escherichia coli strain M15
recombinant MAT II purified by a method that includes Ni-agarose bead affinity capture. Alternative method includes Triton X-100 and 8 mM urea buffered extraction of inclusion body phase and dialysis
-
recombinant protein
three isoforms: MAT-I, MAT-II and MAT-III, MAT-III to homogeneity
-
two isoenzymes: I and II
-
two isoforms: A and B
-
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