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Literature summary for 2.5.1.6 extracted from

  • Ohren, J.; Parungao, G.G.; Viola, R.E.
    Structure of a critical metabolic enzyme S-adenosylmethionine synthetase from Cryptosporidium parvum (2019), Acta Crystallogr. Sect. F, 75, 290-298 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development the enzyme form has a less extensive subunit interface than some previously determined structures, and contains some key structural differences from the human enzyme in an allosteric site, presenting an opportunity for the design of selective inhibitors against the S-adenosylmethionine synthetase from this organism Cryptosporidium parvum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cryptosporidium parvum

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method at 20°C Cryptosporidium parvum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + H2O Cryptosporidium parvum
-
phosphate + diphosphate + S-adenosyl-L-methionine
-
?
ATP + L-methionine + H2O Cryptosporidium parvum Iowa II
-
phosphate + diphosphate + S-adenosyl-L-methionine
-
?

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum Q5CYE4
-
-
Cryptosporidium parvum Iowa II Q5CYE4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cryptosporidium parvum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + H2O
-
Cryptosporidium parvum phosphate + diphosphate + S-adenosyl-L-methionine
-
?
ATP + L-methionine + H2O
-
Cryptosporidium parvum Iowa II phosphate + diphosphate + S-adenosyl-L-methionine
-
?

Synonyms

Synonyms Comment Organism
AdoMet synthetase
-
Cryptosporidium parvum
MetK
-
Cryptosporidium parvum
S-adenosylmethionine synthetase
-
Cryptosporidium parvum

General Information

General Information Comment Organism
metabolism S-adenosyl-L-methionine (AdoMet) is the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism Cryptosporidium parvum