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Literature summary for 2.8.1.11 extracted from

  • Matthies, A.; Nimtz, M.; Leimkühler, S.
    Molybdenum cofactor biosynthesis in humans: Identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry (2005), Biochemistry, 44, 7912-7920.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C316A/C324A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Homo sapiens
C316A/C324A/C365A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Homo sapiens
C412A site-directed mutagenesis, exchange of the conserved active site loop residue, inactive mutant Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[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

Organism UniProt Comment Textmining
Homo sapiens O95396
-
-

Reaction

Reaction Comment Organism Reaction ID
[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine + reduced acceptor = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + [cysteine desulfurase]-L-cysteine + oxidized acceptor double displacement mechanism that requires the transient formation of a stable persulfide-containing intermediate Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[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
-
?
[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine the persulfide group that is exclusively formed on C412, the other three cyteine residues are not involved in sulfur transfer, mass spectrometric analysis, overview. A disulfide bridge between C316 and C324 is not essential for sulfur transfer in vitro Homo sapiens AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase
-
?

Synonyms

Synonyms Comment Organism
MOCS3
-
Homo sapiens
MOCS3-RLD
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
assay at Homo sapiens

General Information

General Information Comment Organism
additional information the recombinant His6-tagged MOCS3-RLD is partially gluconoylated at the N-terminus which results in a heterogeneity of the protein but does not influence sulfurtransferase activity Homo sapiens
physiological function the human MOCS3 protein contains a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of the smaller subunit of molybdopterin, MPT, synthase during molybdenum cofactor biosynthesis in humans. The N-terminus of MOCS3 is expected to activate the C-terminal glycine of, MOCS2A to form an acyl adenylate. Subsequently, the C-terminal rhodanese-like domain (RLD) of MOCS3 acts as a direct sulfur donor for the formation of a thiocarboxylate group on MOCS2A, The MOCS2A thiocarboxylate sulfur is used for the generation of the dithiolene moiety of molybdopterin which coordinates the molybdenum atom in molybdenum cofactor. The enzyme is able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z Homo sapiens