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Information on EC 2.8.1.11 - molybdopterin synthase sulfurtransferase and Organism(s) Homo sapiens

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EC Tree
IUBMB 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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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
molybdenum cofactor biosynthesis protein, mocs3-rld, mocs3 rhodanese-like domain, molybdopterin synthase sulfurylase, molybdopterin synthase sulfurase, cnxf protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOCS3
MOCS3 rhodanese-like domain
-
molybdenum cofactor biosynthesis protein
-
molybdenum cofactor synthesis protein 3
-
-
molybdopterin synthase sulfurase
-
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]-L-cysteine + oxidized acceptor
show the reaction diagram
double displacement mechanism that requires the transient formation of a stable persulfide-containing intermediate
PATHWAY SOURCE
PATHWAYS
-
-
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.
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
?
-
NATURAL SUBSTRATE
NATURAL 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
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
mutation of the putative persulfide-forming active-site cysteine residue C412 abolishes the sulfurtransferase activity of MOCS3-RLD completely
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
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOCS3_HUMAN
460
0
49669
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tagged wild-type and mutant MOCS3 rhodanese-like domain, MOCS3-RLD, from Escherichia coli strain BL21(DE3) by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team