IUBMB Enzyme Nomenclature


Accepted name: molybdopterin synthase sulfurtransferase

Reaction: [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

For diagram of reaction click here.

Other name(s): adenylyltransferase and sulfurtransferase MOCS3; Cnx5 (gene name); molybdopterin synthase sulfurylase

Systematic name: persulfurated L-cysteine desulfurase:[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly sulfurtransferase

Comments: The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC, molybdopterin synthase. In the human, the reaction is catalysed by the rhodanese-like C-terminal domain (cf. EC of the MOCS3 protein, a bifunctional protein that also contains EC, molybdopterin-synthase adenylyltransferase, at the N-terminal domain.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc PDB, CAS registry number:


1. Matthies, A., Nimtz, M. and Leimkuhler, S. Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. Biochemistry 44 (2005) 7912-7920. [PMID: 15910006]

2. Leimkuhler, S. and Rajagopalan, K.V. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J. Biol. Chem. 276 (2001) 22024-22031. [PMID: 11290749]

3. Hanzelmann, P., Dahl, J.U., Kuper, J., Urban, A., Muller-Theissen, U., Leimkuhler, S. and Schindelin, H. Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains. Protein Sci. 18 (2009) 2480-2491. [PMID: 19798741]

4. Dahl, J.U., Urban, A., Bolte, A., Sriyabhaya, P., Donahue, J.L., Nimtz, M., Larson, T.J. and Leimkuhler, S. The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli. J. Biol. Chem. 286 (2011) 35801-35812. [PMID: 21856748]

[EC created 2011, modified 2016]

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