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Literature summary for 4.6.1.17 extracted from

  • Hover, B.M.; Lilla, E.A.; Yokoyama, K.
    Mechanistic investigation of cPMP synthase in molybdenum cofactor biosynthesis using an uncleavable substrate analogue (2015), Biochemistry, 54, 7229-7236 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-P-CH2-PP compound is converted to an analogue of the MoaC reaction intermediate and causes mechanism-based inhibition. the reaction product harbors an acid-labile triaminopyrimidinone base without an established pyranopterin structure and forms a tight complex with MoaC likely through a covalent linkage Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(8S)-3',8-cyclo-7,8-dihydroguanosine-P[CH2]PP
-
Escherichia coli cyclic pyranopterin phosphate + diphosphate
-
?

Synonyms

Synonyms Comment Organism
MoaC
-
Escherichia coli