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Information on EC 2.8.1.11 - molybdopterin synthase sulfurtransferase
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EC Tree
2.8.1.11 molybdopterin synthase sulfurtransferaseIUBMB Comments
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.
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Word Map
- 2.8.1.11
- moco
-
thiocarboxylate
-
mocs2a
-
molybdoenzymes
- thiosulfate
- persulfide
-
gephyrin
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
+
+
+
+
=
+
+
[cysteine desulfurase]-L-cysteine
+
oxidized acceptor
Synonyms
molybdenum cofactor biosynthesis protein, mocs3-rld, mocs3 rhodanese-like domain, molybdopterin synthase sulfurylase, cnxf protein, molybdopterin synthase sulfurase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MOCS3
molybdopterin synthase sulfurylase
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REACTION
REACTION DIAGRAM
COMMENTARY
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]-L-cysteine + oxidized acceptor
[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]-L-cysteine + oxidized acceptor
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-
-
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[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]-L-cysteine + oxidized acceptor
double displacement mechanism that requires the transient formation of a stable persulfide-containing intermediate
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
[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
-
-
-
-
?
[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
-
-
-
?
[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
-
-
-
-
?
[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
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-
-
?
[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
the persulfide group that is exclusively formed on C412, the other three cyteine residues are not involved in sulfur transfer, mass spectrometric analysis, overview. A disulfide bridge between C316 and C324 is not essential for sulfur transfer in vitro
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-
?
additional information
?
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formation of a defined in vitro system consisting of MPT synthase, MoeB, Mg-ATP, IscS, L-cysteine, and YnjE, overview
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-
?
additional information
?
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MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3
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-
?
additional information
?
-
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MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3
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-
?
additional information
?
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MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3
-
-
?
additional information
?
-
-
MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3
-
-
?
additional information
?
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MOCS3 and the MOCS3 rhodanese-like domain, MOCS3-RLD, are also capable to catalyze the transfer of sulfur from thiosulfate to cyanide and shows dithiothreitol:thiosulfate oxidoreductase activity, kinetics, overview
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-
?
additional information
?
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MOCS3 and the MOCS3 rhodanese-like domain, MOCS3-RLD, are also capable to catalyze the transfer of sulfur from thiosulfate to cyanide and shows dithiothreitol:thiosulfate oxidoreductase activity, kinetics, overview
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-
?
additional information
?
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the MOCS3 rhodanese-like domain, MOCS3-RLD, is also capable to catalyze the transfer of sulfur from thiosulfate to cyanide and shows dithiothreitol:thiosulfate oxidoreductase activity, kinetics, overview
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-
?
additional information
?
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the MOCS3 rhodanese-like domain, MOCS3-RLD, is also capable to catalyze the transfer of sulfur from thiosulfate to cyanide and shows dithiothreitol:thiosulfate oxidoreductase activity, kinetics, overview
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-
?
additional information
?
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the MOCS3 rhodanese-like domain, MOCS3-RLD, is also capable to catalyze the transfer of sulfur from thiosulfate to cyanide. Recombinant MOCS3 can activate MOCS2A but not endogenous Escherichia coli MoaD. MOCS3 exhibits sulfurtransferase activity only with thiosulfate, clearly identifying the enzyme as thiosulfate sulfurtransferase. The thiosulfate sulfurtransferase activity of the separated MOCS3-RLD protein is comparable to that of intact MOCS3
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-
?
additional information
?
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the MOCS3 rhodanese-like domain, MOCS3-RLD, is also capable to catalyze the transfer of sulfur from thiosulfate to cyanide. Recombinant MOCS3 can activate MOCS2A but not endogenous Escherichia coli MoaD. MOCS3 exhibits sulfurtransferase activity only with thiosulfate, clearly identifying the enzyme as thiosulfate sulfurtransferase. The thiosulfate sulfurtransferase activity of the separated MOCS3-RLD protein is comparable to that of intact MOCS3
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-
?
additional information
?
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the two-domain protein MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A by its C-terminal rhodanese-like domain (RLD), low activity ofMOCS3-RLD with thiosulfate as sulfur donor
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-
?
additional information
?
-
-
the two-domain protein MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A by its C-terminal rhodanese-like domain (RLD), low activity ofMOCS3-RLD with thiosulfate as sulfur donor
-
-
?
additional information
?
-
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the enzyme interacts with tRNA thiouridine modification protein TUM1
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
[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
-
-
-
-
?
[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
-
-
-
?
[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
-
-
-
-
?
[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
-
-
-
?
additional information
?
-
MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3
-
-
?
additional information
?
-
-
MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3
-
-
?
additional information
?
-
MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3
-
-
?
additional information
?
-
-
MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Molecular characterization of novel immunodominant molybdenum cofactor biosynthesis protein C1 (Rv3111) from Mycobacterium tuberculosis H37Rv.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics of dithiothreitol:thiosulfate oxidoreductase activity and thiosulfate:cyanide sulfurtransferase activity
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additional information
additional information
-
kinetics of dithiothreitol:thiosulfate oxidoreductase activity and thiosulfate:cyanide sulfurtransferase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
8.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
malfunction
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in the moeBA228T mutant strain F36, anaerobic respiratory growth is possible on nitrate but not on DMSO, the cofactor insertion mutation affects the respiratory membrane-bound molybdoenzyme nitrate reductase A (NarGHI), but not respiratory membrane-bound molybdoenzyme dimethylsulfoxide reductase (DmsABC)
malfunction
mutation of the putative persulfide-forming active-site cysteine residue C412 abolishes the sulfurtransferase activity of MOCS3-RLD completely
malfunction
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the moeB mutant of Escherichia coli contains inactive MPT synthase devoid of the thiocarboxylate
metabolism
-
the enzyme catalyzes the second step of the molybdenum cofactor (Moco) biosynthesis
metabolism
the enzyme is involved in the biosynthesis of the molybdenum cofactor divided into three steps: conversion of GTP to precursor, transformation of the precursor to molybdopterin, and insertion of molybdenum into MPT to form the molybdenum cofactor
metabolism
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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
physiological function
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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
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
physiological function
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MoeB functions to sulfurylate MoaD, and in the structure of the MoeB-MoaD complex, Ala228 is located in the interface region between the two proteins
physiological function
molybdopterin synthase sulfurase is involved in sulfur transfer to the C-terminus of the molybdopterin synthase, which synthesizes the molybdenum cofactor, that play a central role in several enzymes, role of specific conserved residues in the six amino acid active site loop of MOCS3-RLD in thiosulfate sulfurtransferase activity
physiological function
-
te enzyme is required for the conversion of precursor Z to molybdopterin
physiological function
the E1-catalyzed activation of the ubiquitin-like protein resembles the second step of the molybdenum cofactor (Moco) biosynthesis in humans and bacteria. For Moco biosynthesis in humans, the E1-like protein MOCS3 forms a thiocarboxylate group at the C-terminal glycine of the beta-grasp fold protein MOCS2A. molybdenum cofactor biosynthesis and tRNA thiolation steps are linked by the MOCS3 protein in humans, mechanism of protein conjugation and thiocarboxylate formation in sulfur transfer pathways, overview
physiological function
the human MOCS3 gene encodes a protein involved in activation and sulfuration of the C-terminus of MOCS2A, the smaller subunit of the molybdopterin (MPT) synthase. MPT synthase catalyzes the formation of the dithiolene group of MPT that is required for the coordination of the molybdenum atom in the last step of molybdenum cofactor (Moco) biosynthesis. The L-cysteine desulfurase Nfs1 might be involved in the sulfuration ofMOCS3 in vivo. Sulfur transfer mechanism, overview
physiological function
the human MOCS3 protein contains a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of the smaller subunit of molybdopterin, MPT, synthase during molybdenum cofactor biosynthesis in humans. The N-terminus of MOCS3 is expected to activate the C-terminal glycine of, MOCS2A to form an acyl adenylate. Subsequently, the C-terminal rhodanese-like domain (RLD) of MOCS3 acts as a direct sulfur donor for the formation of a thiocarboxylate group on MOCS2A, The MOCS2A thiocarboxylate sulfur is used for the generation of the dithiolene moiety of molybdopterin which coordinates the molybdenum atom in molybdenum cofactor. The enzyme is able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z
physiological function
the MOCS3 protein is believed to catalyze both the adenylation and the subsequent generation of a thiocarboxylate group at the C terminus of the smaller subunit of molybdopterin (MPT) synthase, the C-terminal segment of MOCS3 displays similarities to the sulfurtransferase rhodanese. The MOCS3 rhodanese-like domain provides the sulfur for the thiocarboxylation of MOCS2A, the small MPT synthase subunit in humans. C412 is important for catalysis. The MoeB domain of MOCS3 is not involved in sulfur transfer in vitro
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
additional information
-
maturation of the holoenzyme is not cofactor-insertion dependent
additional information
MOCS3 interacts with both URM1, an ubiquitin-like modifier involved in the specific formation of 2-thiouridine tRNA in humans, and MOCS2A in vivo and in vitro, MOCS2A and URM1 are beta-grasp fold proteins that contain a highly conserved C-terminal double glycine motif. Deletion of the C-terminal glycine of either MOCS2A or URM1 results in a loss of interaction with MOCS3. Extension of the C-terminus with an additional glycine of MOCS2A and URM1 alters the localization of MOCS3from the cytosol to the nucleus
additional information
-
MOCS3 interacts with both URM1, an ubiquitin-like modifier involved in the specific formation of 2-thiouridine tRNA in humans, and MOCS2A in vivo and in vitro, MOCS2A and URM1 are beta-grasp fold proteins that contain a highly conserved C-terminal double glycine motif. Deletion of the C-terminal glycine of either MOCS2A or URM1 results in a loss of interaction with MOCS3. Extension of the C-terminus with an additional glycine of MOCS2A and URM1 alters the localization of MOCS3from the cytosol to the nucleus
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
additional information
Nfs1 interacts specifically with MOCS3-RLD and sulfur is transferred from L-cysteine to MOCS3-RLD via an Nfs1-bound persulfide intermediate. Cytosolic Nfs1 has an important role in sulfur transfer for the biosynthesis of Moco. Isd11 functions as an adapter and stabilizer of Nfs1. Sulfur transfer mechanism, overview
additional information
-
Nfs1 interacts specifically with MOCS3-RLD and sulfur is transferred from L-cysteine to MOCS3-RLD via an Nfs1-bound persulfide intermediate. Cytosolic Nfs1 has an important role in sulfur transfer for the biosynthesis of Moco. Isd11 functions as an adapter and stabilizer of Nfs1. Sulfur transfer mechanism, overview
additional information
-
the enzyme contains two potential nucleotide binding Gly-rich motifs (Gly-X-Gly-X-X-Gly) starting at residue positions 173 and 189
additional information
the MOCS3 C-terminal domain is homologous to rhodanese-like proteins. The last amino acid must be either polar or positively charged to increase the thiosulfate sulfurtransferase activity of MOCS3-RLD
additional information
-
the MOCS3 C-terminal domain is homologous to rhodanese-like proteins. The last amino acid must be either polar or positively charged to increase the thiosulfate sulfurtransferase activity of MOCS3-RLD
additional information
the recombinant His6-tagged MOCS3-RLD is partially gluconoylated at the N-terminus which results in a heterogeneity of the protein but does not influence sulfurtransferase activity
additional information
-
the recombinant His6-tagged MOCS3-RLD is partially gluconoylated at the N-terminus which results in a heterogeneity of the protein but does not influence sulfurtransferase activity
Show AA Sequence and Transmembrane Helices (1415 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the 158 C-terminal amino acids form the MOCS3 rhodanese-like domain, MOCS3-RLD
additional information
-
the 158 C-terminal amino acids form the MOCS3 rhodanese-like domain, MOCS3-RLD
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A228T
-
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
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C316A/C324A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C316A/C324A/C365A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C324A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C365A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
C412A
D417R
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
site-directed mutagenesis, the mutant shows a 17fold increased dithiothreitol:thiosulfate oxidoreductase activity or a 90fold increased thiosulfate:cyanide sulfurtransferase activity
G415A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K413R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L414K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N416V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P458G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y460A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
C412A
site-directed mutagenesis, exchange of the conserved active site loop residue, inactive mutant
C412A
-
site-directed mutagenesis, exchange of the conserved active site loop residue, inactive mutant
additional information
-
generation of several hundred cnx mutants by radom mutagenesis, activity analysis and phenotypes, overview
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
additional information
when the six amino acid active site loop of MOCS3 rhodanese-like domain is exchanged with the loop found in bovine rhodanese, thiosulfate:cyanide sulfurtransferase activity is increased 165fold. By site-directed mutagenesis also the whole loop is exchanged with the one found in bovine rhodanese, which results in a 36fold increase in the kcat with dithiothreitol in the assay mixture and a 165fold increased kcat with cyanide as sulfur acceptor
additional information
-
when the six amino acid active site loop of MOCS3 rhodanese-like domain is exchanged with the loop found in bovine rhodanese, thiosulfate:cyanide sulfurtransferase activity is increased 165fold. By site-directed mutagenesis also the whole loop is exchanged with the one found in bovine rhodanese, which results in a 36fold increase in the kcat with dithiothreitol in the assay mixture and a 165fold increased kcat with cyanide as sulfur acceptor
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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
-
recombinant N-terminally TAP-tagged MoeB from Escherichia coli strain CL100(DE3) (DELTAiscS) by protein G affinity chromatography
-
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
-
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)
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sambasivarao, D.; Turner, R.; Bilous, P.; Rothery, R.; Shaw, G.; Weiner, J.
Differential effects of a molybdopterin synthase sulfurylase (moeB) mutation on Escherichia coli molybdoenzyme maturation
Biochem. Cell Biol.
80
435-443
2002
Escherichia coli
brenda
Matthies, A.; Nimtz, M.; Leimkhler, S.
Molybdenum cofactor biosynthesis in humans: Identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry
Biochemistry
44
7912-7920
2005
Homo sapiens (O95396), Homo sapiens
brenda
Krepinsky, K.; Leimkuehler, S.
Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs
FEBS J.
274
2778-2787
2007
Homo sapiens (O95396), Homo sapiens
brenda
Appleyard, M.V.C.L.; Sloan, J.; Kanan, G.; Heck, I.; Kinghorn, J.; Unkles, S.
The Aspergillus nidulans cnxF gene and its involvement in molybdopterin biosynthesis: molecular characterization and analysis of in vivo generated mutants
J. Biol. Chem.
273
14869-14876
1998
Aspergillus nidulans
brenda
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
J. Biol. Chem.
276
22024-22031
2001
Escherichia coli
brenda
Marelja, Z.; Stoecklein, W.; Nimtz, M.; Leimkhler, S.
A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
J. Biol. Chem.
283
25178-25185
2008
Homo sapiens (O95396), Homo sapiens
brenda
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
J. Biol. Chem.
286
35801-35812
2011
Escherichia coli
brenda
Chowdhury, M.; Dosche, C.; Lhmannsrben, H.; Leimkhler, S.
Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans
J. Biol. Chem.
287
17297-17307
2012
Homo sapiens (O95396), Homo sapiens
brenda
Matthies, A.; Rajagopalan, K.; Mendel, R.; Leimkhler, S.
Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans
Proc. Natl. Acad. Sci. USA
101
5946-5951
2004
Homo sapiens (O95396), Homo sapiens
brenda
Fraesdorf, B.; Radon, C.; Leimkuehler, S.
Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans
J. Biol. Chem.
289
34543-34556
2014
Homo sapiens
brenda
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