Information on EC 2.8.1.11 - molybdopterin synthase sulfurtransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.8.1.11
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RECOMMENDED NAME
GeneOntology No.
molybdopterin synthase sulfurtransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine + reduced acceptor = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + [cysteine desulfurase] + oxidized acceptor
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
molybdenum cofactor biosynthesis
SYSTEMATIC NAME
IUBMB Comments
[cysteine desulfurase]-S-sulfanyl-L-cysteine:[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly sulfurtransferase
The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC 2.8.1.12, molybdopterin synthase. In the human, the reaction is catalysed by the rhodanese-like C-terminal domain (cf. EC 2.8.1.1) of the MOCS3 protein, a bifunctional protein that also contains EC 2.7.7.80, molybdopterin-synthase adenylyltransferase, at the N-terminal domain.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cnxF
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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MOCS3 belongs to the class of rhodaneses that is found in combination with another protein domain, and contains one rhodanese domain of 158 amino acids at the C-terminus with a sequence identity of less than 20% with the classic two-domain rhodaneses, phylogenetic analysis of MoeB homologues, overview
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[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
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[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
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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MoaD binds to MoeB only in the presence of ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
IscS protein
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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
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YnjE protein
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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kinetics of dithiothreitol:thiosulfate oxidoreductase activity and thiosulfate:cyanide sulfurtransferase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
8.6
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
25
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assay at
30
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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cytoplasmic membranes
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the 158 C-terminal amino acids form the MOCS3 rhodanese-like domain, MOCS3-RLD
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant MoeB from Echerichia coli strain moaD2(DE3) by ammonium sulfate fractionation, ion exchange chromatography, hydrophobic interaction chromatography, and gel filtration
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recombinant N-terminally TAP-tagged MoeB from Escherichia coli strain CL100(DE3) (DELTAiscS) by protein G affinity chromatography
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recombinant tagged wild-type and mutant MOCS3 rhodanese-like domain, MOCS3-RLD, from Escherichia coli strain BL21(DE3) by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cnxF, DNA and amino acid sequence determination and analysis, sequence comparison, genetic structure and organization
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gene moeB, DNA and amino acid sequence determination and analysis
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gene moeB, expression in Escherichia coli strain moaD2(DE3)
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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)
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MOCS3 is encoded by an intronless gene located on chromosome 20, expression of wild-type and mutant tagged MOCS3 rhodanese-like domain, MOCS3-RLD, in Escherichia coli strain BL21(DE3)
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phylogenetic analysis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G160D
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radom mutagenesis, temperature-sensitive phenotype
G178D
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radom mutagenesis, temperature-sensitive phenotype
G342S
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radom mutagenesis., temperature-sensitive phenotype
A228T
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random mutagenesis, from mutant strain F36, the chromosomal mutant of moeB demonstrates limited molybdenum cofactor molybdo-bis(molybdopterin guanine dinucleotide) availability in Escherichia coli, the moeBA228T mutation disrupts the interaction between MoeB and MoaD. The mutant is defective in anaerobic respiration and growth on DMSO
C316A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C316A/C324A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C316A/C324A/C365A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C324A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C365A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C412A
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site-directed mutagenesis, exchange of the conserved active site loop residue, inactive mutant
D417R
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site-directed mutagenesis, the kcat of the mutant variant is increased 83fold when dithiothreitol is used as reductant, or 470fold when cyanide is used as sulfur acceptor
D417T
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site-directed mutagenesis, the mutant shows a 17fold increased dithiothreitol:thiosulfate oxidoreductase activity or a 90fold increased thiosulfate:cyanide sulfurtransferase activity
G415A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K413R
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L414K
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N416V
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P458G
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y460A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
Show AA Sequence (711 entries)
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