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EC 2.8.1.12 Details

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EC number

2.8.1.12

Accepted name

molybdopterin synthase

Reaction

cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH₂-C(O)SH + H₂O = molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein

Other name(s)

MPT synthase

Systematic name

thiocarboxylated molybdopterin synthase:cyclic pyranopterin phosphate sulfurtransferase

Comment

Catalyses the synthesis of molybdopterin from cyclic pyranopterin monophosphate. Two sulfur atoms are transferred to cyclic pyranopterin monophosphate in order to form the characteristic ene-dithiol group found in the molybdenum cofactor. Molybdopterin synthase consists of two large subunits forming a central dimer and two small subunits (molybdopterin-synthase sulfur-carrier proteins) that are thiocarboxylated at the C-terminus by EC 2.8.1.11, molybdopterin synthase sulfurtransferase. The reaction occurs in prokaryotes and eukaryotes.

History

created 2011

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.12.1 With NAD⁺ or NADP⁺ as acceptor

1.12.2 With a cytochrome as acceptor

1.12.5 With a quinone or similar compound as acceptor

1.12.7 With an iron-sulfur protein as acceptor

1.12.98 With other, known, physiological acceptors

1.12.99 With unknown physiological acceptors

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.13.1. undefined

1.13.11 With incorporation of two atoms of oxygen

1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

1.13.99 Miscellaneous

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

2.1 Transferring one-carbon groups

2.2 Transferring aldehyde or ketonic groups

2.3 Acyltransferases

2.4 Glycosyltransferases

2.5 Transferring alkyl or aryl groups, other than methyl groups

2.6 Transferring nitrogenous groups

2.7 Transferring phosphorus-containing groups

2.8 Transferring sulfur-containing groups

2.8.1 Sulfurtransferases

2.8.1.1 thiosulfate sulfurtransferase

2.8.1.2 3-mercaptopyruvate sulfurtransferase

2.8.1.3 thiosulfate—thiol sulfurtransferase

2.8.1.4 tRNA uracil 4-sulfurtransferase

2.8.1.5 thiosulfate—dithiol sulfurtransferase

2.8.1.6 biotin synthase

2.8.1.7 cysteine desulfurase

2.8.1.8 lipoyl synthase

2.8.1.9 molybdenum cofactor sulfurtransferase

2.8.1.10 thiazole synthase

2.8.1.11 molybdopterin synthase sulfurtransferase

2.8.1.12 molybdopterin synthase

2.8.1.13 tRNA-uridine 2-sulfurtransferase

2.8.1.14 tRNA-5-taurinomethyluridine 2-sulfurtransferase

2.8.1.15 tRNA-5-methyluridine⁵⁴ 2-sulfurtransferase

2.8.1.16 L-aspartate semialdehyde sulfurtransferase

2.8.2 Sulfotransferases

2.8.3 CoA-transferases

2.8.4 Transferring alkylthio groups

2.8.5 Thiosulfotransferases

2.9 Transferring selenium-containing groups

2.10 Transferring molybdenum- or tungsten-containing groups

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Release 2023.1 (January 2023)