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Information on EC 4.6.1.17 - cyclic pyranopterin monophosphate synthase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaC and Cnx3, respectively. In mammals the reaction is catalysed by the MOCS1B domain of the bifuctional MOCS1 protein, which also catalyses EC 4.1.99.22, GTP 3',8-cyclase.
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
moac2, st0472, molybdenum cofactor biosynthesis protein c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cnx3
-
-
-
-
MoaC
-
-
-
-
MOCS1B
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate lyase (cyclic pyranopterin phosphate-forming)
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaC and Cnx3, respectively. In mammals the reaction is catalysed by the MOCS1B domain of the bifuctional MOCS1 protein, which also catalyses EC 4.1.99.22, GTP 3',8-cyclase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOCS1_HUMAN
636
0
70105
Swiss-Prot
Mitochondrion (Reliability: 1)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the first two enzymes of the molybdopterin biosynthesis pathway are encoded by the MOCS1 locus in humans. Isoform MOCS1A and isoform MOCS1B form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate. They are encoded by an apparently bicistronic MOCS1AMOCS1B transcript which bypasses the normal termination nonsense codon of MOCS1A resulting in fusion of the MOCS1A and MOCS1B open reading frames. The bicistronic form of MOCS1 mRNA is likely to only produce MOCS1A protein and suggests that MOCS1B is translated only as a fusion with MOCS1A
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gray, T.A.; Nicholls, R.D.
Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames
RNA
6
928-936
2000
Homo sapiens (Q9NZB8)
Manually annotated by BRENDA team