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Literature summary for 4.1.99.22 extracted from

  • Hänzelmann, P.; Hernandez, H.L.; Menzel, C.; Garcia-Serres, R.; Huynh, B.H.; Johnson, M.K.; Mendel, R.R.; Schindelin, H.
    Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis (2004), J. Biol. Chem., 279, 34721-34732.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
iron-sulfur centre contains two oxygen-sensitive FeS clusters, each coordinated by only three cysteine residues. A redox-active [4Fe-4S]2+,+cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S]0 cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+clusters. The N-terminal [4Fe-4S]2+cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S]0 cluster intermediate Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP Homo sapiens the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor cyclic pyranopterin phosphate + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP
-
 Homo sapiens cyclic pyranopterin phosphate + diphosphate
-
 ?
GTP the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor Homo sapiens cyclic pyranopterin phosphate + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
MOCS1A
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre contains two oxygen-sensitive FeS clusters, each coordinated by three cysteine residues. A redox-active [4Fe-4S]2+ cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S] cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+ clusters. The N-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S] cluster intermediate Homo sapiens