Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
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 | Comment | Organism |
---|---|---|
MOCS1A | - |
Homo sapiens |
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 |