Molybdopterin synthase sulfurtransferase

Molybdopterin synthase sulfurtransferase
Identifiers
EC number 2.8.1.11
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Molybdopterin synthase sulfurtransferase (EC 2.8.1.11, adenylyltransferase and sulfurtransferase MOCS3, Cnx5 (gene), molybdopterin synthase sulfurylase) is an enzyme with systematic name persulfurated L-cysteine desulfurase:(molybdopterin-synthase sulfur-carrier protein)-Gly-Gly sulfurtransferase.[1][2][3][4] This enzyme catalyses the following chemical reaction

[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase

The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of molybdopterin synthase.

References

  1. Matthies, A.; Nimtz, M.; Leimkuhler, S. (2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44: 7912–7920. doi:10.1021/bi0503448. PMID 15910006.
  2. Leimkuhler, S.; Rajagopalan, K.V. (2001). "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 (25): 22024–22031. doi:10.1074/jbc.M102072200. PMID 11290749.
  3. Hanzelmann, P.; Dahl, J.U.; Kuper, J.; Urban, A.; Muller-Theissen, U.; Leimkuhler, S.; Schindelin, H. (2009). "Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains". Protein Sci. 18 (12): 2480–2491. doi:10.1002/pro.260. PMID 19798741.
  4. Dahl, J.U.; Urban, A.; Bolte, A.; Sriyabhaya, P.; Donahue, J.L.; Nimtz, M.; Larson, T.J.; Leimkuhler, S. (2011). "The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli". J. Biol. Chem. 286 (41): 35801–35812. doi:10.1074/jbc.M111.282368. PMID 21856748.
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