Literature summary for 2.8.1.11 extracted from

Leimkuehler, S.; 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 (2001), J. Biol. Chem., 276, 22024-22031.

Search for more literature for 2.8.1.11

Cloned(Commentary)

Cloned (Comment)	Organism
gene moeB, expression in Escherichia coli strain moaD2(DE3)	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	development of a fully defined in vitro system in which an inactive form of MPT synthase can be activated by incubation with MoeB, Mg-ATP, L-cysteine, and one of the NifS-like sulfurtransferases, and the addition of precursor Z to the in vitro system gives rise to MPT formation	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

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	Escherichia coli	-	AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	gene moeB	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant MoeB from Echerichia coli strain moaD2(DE3) by ammonium sulfate fractionation, ion exchange chromatography, hydrophobic interaction chromatography, and gel filtration	Escherichia coli

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	-	Escherichia coli	AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + cysteine desulfurase	-	?

Synonyms

Synonyms	Comment	Organism
MoeB	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Escherichia coli

General Information

General Information	Comment	Organism
malfunction	the moeB mutant of Escherichia coli contains inactive MPT synthase devoid of the thiocarboxylate	Escherichia coli
metabolism	the enzyme is involved in the biosynthesis of the molybdenum cofactor, catalyzing the transfer of the sulfur atom of the C-terminal thiocarboxylate from the small subunit of the synthase to generate the dithiolene group of MPT. After the transfer of sulfur from MPT synthase to precursor Z, MPT synthase is present in an inactive, desulfurated form lacking the C-terminal thiocarboxylate group at the MoaD subunit of the protein	Escherichia coli
additional information	L-cysteine can serve as the source of the sulfur for the biosynthesis of MPT in vitro but only in the presence of a persulfide-containing sulfurtransferase such as IscS, cysteine sulfinate desulfinase (CSD), or CsdB. But IscS is not required for the in vivo sulfuration of MPT synthase. Development of a fully defined in vitro system in which an inactive form of MPT synthase can be activated by incubation with MoeB, Mg-ATP, L-cysteine, and one of the NifS-like sulfurtransferases, and the addition of precursor Z to the in vitro system gives rise to MPT formation, overview. Three NifS-like sulfurtransferases can catalyze the activation of MPT synthase	Escherichia coli
physiological function	conversion of precursor Z to molybdopterin (MPT) by Escherichia coli MPT synthase entails the transfer of the sulfur atom of the C-terminal thiocarboxylate from the small subunit of the synthase to generate the dithiolene group of MPT. The sulfurtransferase is also required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z. The sulfur is transferred as a protein-bound persulfide	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)