Enzyme

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     4. Lyases
        4.6 Phosphorus-oxygen lyases
            4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
ID:4.6.1.17
Description:Cyclic pyranopterin monophosphate synthase.
Cath: 3.30.70.640;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.6.1.17
BRENDA Enzyme Link: BRENDA 4.6.1.17
KEGG Enzyme Link: KEGG4.6.1.17
BioCyc Enzyme Link: BioCyc 4.6.1.17
ExPASy Enzyme Link: ExPASy4.6.1.17
EC2PDB Enzyme Link: EC2PDB 4.6.1.17
ExplorEnz Enzyme Link: ExplorEnz 4.6.1.17
PRIAM enzyme-specific profiles Link: PRIAM 4.6.1.17
IntEnz Enzyme Link: IntEnz 4.6.1.17
MEDLINE Enzyme Link: MEDLINE 4.6.1.17
MSA:

4.6.1.17;

Phylogenetic Tree:

4.6.1.17;

Uniprot:
M-CSA:
RHEA:49580 (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
RULE(radius=1)
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis.Hover BM, Tonthat NK, Schumacher MA, Yokoyama K2015 May 1925941396
C-Terminal glycine-gated radical initiation by GTP 3',8-cyclase in the molybdenum cofactor biosynthesis.Hover BM, Yokoyama K2015 Mar 1125697423
Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis.Hover BM, Loksztejn A, Ribeiro AA, Yokoyama K2013 May 823627491
Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors.Rieder C, Eisenreich W, O'Brien J, Richter G, Götze E, Boyle P, Blanchard S, Bacher A, Simon H1998 Jul 19692897
Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies.Wuebbens MM, Rajagopalan KV1995 Jan 207836363
The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor.Santamaria-Araujo JA, Fischer B, Otte T, Nimtz M, Mendel RR, Wray V, Schwarz G2004 Apr 1614761975