Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Minici, C.; Mosca, L.; Ilisso, C.P.; Cacciapuoti, G.; Porcelli, M.; Degano, M.
    Structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues (2020), J. Struct. Biol., 210, 107462 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.6 expression in Escherichia coli Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.6 hanging drop vapour diffusion method, structural analysis of the Pyrococcus furiosus methionine adenosyltransferase captured in the unliganded, substrate-and product-bound states Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.6 ATP + L-methionine + H2O Pyrococcus furiosus the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?
2.5.1.6 ATP + L-methionine + H2O Pyrococcus furiosus ATCC 43587 the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.6 Pyrococcus furiosus Q8TZW1
-
-
2.5.1.6 Pyrococcus furiosus ATCC 43587 Q8TZW1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.6
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.6 ATP + L-methionine + H2O
-
 Pyrococcus furiosus phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?
2.5.1.6 ATP + L-methionine + H2O the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions Pyrococcus furiosus phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?
2.5.1.6 ATP + L-methionine + H2O
-
 Pyrococcus furiosus ATCC 43587 phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?
2.5.1.6 ATP + L-methionine + H2O the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions Pyrococcus furiosus ATCC 43587 phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.6 80
-
 assay at Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.6 8
-
 assay at Pyrococcus furiosus

General Information

EC Number General Information Comment Organism
2.5.1.6 evolution structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues. The distinct molecular mechanism for S-adenosylmethionine synthesis in Archaea is likely consequence of the evolutionary pressure to achieve protein stability under extreme conditions Pyrococcus furiosus
2.5.1.6 metabolism the enzyme catalyse the biosynthesis of S-adenosylmethionine, the primary methyl group donor in biochemical reactions Pyrococcus furiosus