Enzyme

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     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.1 Sulfurtransferases
ID:2.8.1.11
Description:Molybdopterin synthase sulfurtransferase.
Alternative Name: Molybdopterin synthase sulfurylase.
Cath: 3.40.50.720; 3.90.1170.40; 3.40.250.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.1.11
BRENDA Enzyme Link: BRENDA 2.8.1.11
KEGG Enzyme Link: KEGG2.8.1.11
BioCyc Enzyme Link: BioCyc 2.8.1.11
ExPASy Enzyme Link: ExPASy2.8.1.11
EC2PDB Enzyme Link: EC2PDB 2.8.1.11
ExplorEnz Enzyme Link: ExplorEnz 2.8.1.11
PRIAM enzyme-specific profiles Link: PRIAM 2.8.1.11
IntEnz Enzyme Link: IntEnz 2.8.1.11
MEDLINE Enzyme Link: MEDLINE 2.8.1.11
MSA:

2.8.1.11;

Phylogenetic Tree:

2.8.1.11;

Uniprot:
M-CSA:
RHEA:48612 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]
RULE(radius=1) [*:1]-[O;H0;+0:2]-[C;H0;+0:3](-[*:4])=[*:5].[*:6]-[S;H0;+0:7]-[SH;+0:8]>>[*:4]-[C;H0;+0:3](=[*:5])-[SH;+0:8].[*:1]-[OH;+0:2].[*:6]-[SH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.Matthies A, Nimtz M, Leimkühler S2005 May 3115910006
The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli.Dahl JU, Urban A, Bolte A, Sriyabhaya P, Donahue JL, Nimtz M, Larson TJ, Leimkühler S2011 Oct 1421856748
Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains.Hänzelmann P, Dahl JU, Kuper J, Urban A, Müller-Theissen U, Leimkühler S, Schindelin H2009 Dec19798741
A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli.Leimkühler S, Rajagopalan KV2001 Jun 2211290749