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Literature summary extracted from

  • Dahl, J.; Urban, A.; Bolte, A.; Sriyabhaya, P.; Donahue, J.; Nimtz, M.; Larson, T.; Leimkuehler, S.
    The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli (2011), J. Biol. Chem., 286, 35801-35812.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.8.1.11 IscS protein IscS, a three-domain rhodanese-like protein, specifically interacts with YnjE for the formation of the persulfide group on YnjE and enhances the reaction in an in vitro system, consisting of MPT synthase, MoeB, Mg-ATP, IscS, L-cysteine, and YnjE. It also interacts with MoeB. The role of YnjE is to make the sulfur transfer from IscS for Moco biosynthesis more specific, since IscS is involved in a variety of different sulfur transfer reactions in the cell. IscS is the preferred sulfur donor for YnjE in vivo Escherichia coli
2.8.1.11 YnjE protein specifically interacts with IscS for the formation of the persulfide group on YnjE and enhances the reaction in an in vitro system, consisting of MPT synthase, MoeB, Mg-ATP, IscS, L-cysteine, and YnjE. Best activating in a ratio of 1:2 with MPT, is inhibitory at ratio 1:10. It also interacts with MoeB. The role of YnjE is to make the sulfur transfer from IscS for Moco biosynthesis more specific, since IscS is involved in a variety of different sulfur transfer reactions in the cell. IscS is the preferred sulfur donor for YnjE in vivo. Nevertheless YnjE is not a real enhancer of L-cysteine desulfurase activity, but rather leads to a better rate of conversion of cPMP to MPT. YnjE occurs in the cytosol and the periplasm Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.1.11 gene moeB, recombinant expression of MoeB in Escherichia coli strain BL21(DE3), and expression as N-terminally TAP-tagged protein in Escherichia coli strain CL100(DE3) (DELTAiscS) Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.11 [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine Escherichia coli
-
 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 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.1.11 recombinant N-terminally TAP-tagged MoeB from Escherichia coli strain CL100(DE3) (DELTAiscS) by protein G affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.11 additional information formation of a defined in vitro system consisting of MPT synthase, MoeB, Mg-ATP, IscS, L-cysteine, and YnjE, overview Escherichia coli ?
-
 ?
2.8.1.11 [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine
-
 Escherichia coli AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.8.1.11 IscS
-
 Escherichia coli
2.8.1.11 L-cysteine desulfurase
-
 Escherichia coli
2.8.1.11 MoeB
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.1.11 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.1.11 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.1.11 ATP MoaD binds to MoeB only in the presence of ATP Escherichia coli

General Information

EC Number General Information Comment Organism
2.8.1.11 metabolism the enzyme catalyzes the second step of the molybdenum cofactor (Moco) biosynthesis Escherichia coli
2.8.1.11 additional information MoeB-MoaD complex formation by protein-protein interactions, MoaD binds to MoeB only in the presence of ATP, while IscS is not essential for the binding of MoeB to YnjE, IscS and MoeB bind independently to YnjE Escherichia coli
2.8.1.11 physiological function in Escherichia coli, the L-cysteine desulfurase IscS is the primary sulfur donor for the formation of the thiocarboxylate by MoeB on the small subunit (MoaD) of MPT synthase, which catalyzes the conversion of cyclic pyranopterin monophosphate to molybdopterin, MPT. YnjE, a three-domain rhodanese-like protein from Escherichia coli, interacts with MoeB possibly for sulfur transfer to MoaD. Modeling of molybdopterin formation in the complex containing MoeB, MoaaD, MoaE, YnjE, IscC, and AMP, overview Escherichia coli