Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chowdhury, M.; Dosche, C.; Löhmannsröben, H.; Leimkühler, S.
    Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans (2012), J. Biol. Chem., 287, 17297-17307.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.11 additional information Homo sapiens MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3 ?
-
 ?
2.8.1.11 [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine Homo sapiens
-
 AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.11 Homo sapiens O95396
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.11 additional information MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3 Homo sapiens ?
-
 ?
2.8.1.11 additional information MOCS3 and the MOCS3 rhodanese-like domain, MOCS3-RLD, are also capable to catalyze the transfer of sulfur from thiosulfate to cyanide and shows dithiothreitol:thiosulfate oxidoreductase activity, kinetics, overview Homo sapiens ?
-
 ?
2.8.1.11 [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine
-
 Homo sapiens AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.8.1.11 MOCS3
-
 Homo sapiens
2.8.1.11 molybdenum cofactor biosynthesis protein
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.1.11 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.1.11 7.2
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
2.8.1.11 additional information MOCS3 interacts with both URM1, an ubiquitin-like modifier involved in the specific formation of 2-thiouridine tRNA in humans, and MOCS2A in vivo and in vitro, MOCS2A and URM1 are beta-grasp fold proteins that contain a highly conserved C-terminal double glycine motif. Deletion of the C-terminal glycine of either MOCS2A or URM1 results in a loss of interaction with MOCS3. Extension of the C-terminus with an additional glycine of MOCS2A and URM1 alters the localization of MOCS3from the cytosol to the nucleus Homo sapiens
2.8.1.11 physiological function the E1-catalyzed activation of the ubiquitin-like protein resembles the second step of the molybdenum cofactor (Moco) biosynthesis in humans and bacteria. For Moco biosynthesis in humans, the E1-like protein MOCS3 forms a thiocarboxylate group at the C-terminal glycine of the beta-grasp fold protein MOCS2A. molybdenum cofactor biosynthesis and tRNA thiolation steps are linked by the MOCS3 protein in humans, mechanism of protein conjugation and thiocarboxylate formation in sulfur transfer pathways, overview Homo sapiens