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Information on EC 2.8.1.9 - molybdenum cofactor sulfurtransferase
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2.8.1.9 molybdenum cofactor sulfurtransferaseIUBMB Comments
Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 2.8.1.7), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.
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Word Map
- 2.8.1.9
- mocos
-
abscisic
- drought
-
xanthinuria
-
nifs-like
-
transpirational
-
desulfurase
-
wilting
- persulfide
-
amidoxime
- allopurinol
-
aba-deficient
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
+
+
2
=
+
+
+
+
+
+
2
=
+
+
+
oxidized acceptor
Synonyms
ABA3, cysteine desulfurase, LOS5, LOS5/ABA3, MCSU, molybdenum cofactor sulfurase, molybdenum cofactor sulphurase, molybdenum-cofactor sulfurase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LOS5
molybdenum cofactor sulfurase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine:molybdenum cofactor sulfurtransferase
Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 2.8.1.7), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.
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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
L-cysteine
L-alanine + H2S
-
in presence of DTT as reducing agent, activity of the the cysteine desulfurase domain
-
?
L-cysteine methyl ester
L-alanine methyl ester + H2S
-
in presence of DTT as reducing agent, activity of the the cysteine desulfurase domain
-
?
L-selenocysteine
L-alanine + H2Se
-
in presence of DTT as reducing agent, activity of the the cysteine desulfurase domain
-
?
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
-
-
-
?
molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
-
-
-
-
?
molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
the enzyme consists of an N-terminal NifS-like domain that exhibits L-cysteine desulfurase activity and a C-terminal domain that binds sulfurated molybdenum cofactor
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
-
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
-
-
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
-
-
-
?
additional information
?
-
no detectable activity for L-cysteine ethylester, glutathione, beta-mercaptopyruvate, L-cysteamine, and L-cystine
-
-
?
additional information
?
-
-
no detectable activity for L-cysteine ethylester, glutathione, beta-mercaptopyruvate, L-cysteamine, and L-cystine
-
-
?
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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
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
-
-
-
?
molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
-
-
-
-
?
molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
the enzyme consists of an N-terminal NifS-like domain that exhibits L-cysteine desulfurase activity and a C-terminal domain that binds sulfurated molybdenum cofactor
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
-
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
-
-
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
less than 80% activity at 1 mM, 30% activity at 1.5 mM, complete inhibition at 2 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
L-cysteine
for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
0.2
L-selenocysteine
for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
L-cysteine
for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
0.357
L-selenocysteine
for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
molybdenum-cofactor sulfurase is a key regulator of abscisic acid biosynthesis
physiological function
-
enzyme overexpression in transgenic tobacco can enhance drought tolerance. Enzyme overexpressing tobacco seedlings show lower transpirational water loss than that of nontransgenic seedlings in the same period under normal conditions. Transgenic plants show less wilting, maintain higher water content and better cellular membrane integrity, accumulate higher quantities of abscisic acid and proline, and exhibit higher activities of antioxidant enzymes, i.e., superoxide dismutase, catalase, peroxidase and ascorbate peroxidase, as compared with control plants
physiological function
-
overexpression of Arabidopsis molybdenum cofactor sulfurase gene LOS5 in maize markedly enhances the expression and activity of aldehyde oxidase, leading to absisic acid accumulation and increased drought tolerance by decreasing stomatal aperture to reduce water loss. LOS5 overexpression enhances abiotic stress-related genes
physiological function
-
the enzyme is involved in aldehyde oxidase activity in Arabidopsis, which indirectly regulates absisic acid biosynthesis and increases stress tolerance. Overexpression of the enzyme prevents water loss and modulates stomatal closure, enhances expression of stress-upregulated genes and promotes absisic acid accumulation to drought stress. Enzyme overexpression also enhances biomass accumulation and produces higher yield in the field
physiological function
the enzyme enhances the tolerance to high salt, cold, osmotic stresses, and abscisic acid induction
physiological function
endogenous levels of anthocyanins are significantly lower in the ABA3 mutant than in the wild type or an xanthoxin dehydrogenase ABA2 mutant under oxidative stress. Mutants defective in the aldehyde oxidase and xanthine dehydrogenase holoenzymes accumulate significantly higher levels of anthocyanins when compared with the ABA3 mutant under the same conditions
physiological function
overexpression in Sesamum indicum. Under severe drought conditions, transgenic plants show less reduction in height compared to azygous non-transgenic plants. Increase in total extractable soluble proteins, elevation in proline accumulation, and a reduction in MDA levels are recorded in transgenic lines. Under non-stressed conditions, ascorbate peroxidase, catalase, peroxidase and superoxide dismutase activity levels increase by 25%, 23%, 210% and 75%, respectively, compared to azygous non-transgenic plants
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C428/435A
the mutant shows wild type sensitivity towards N-ethylmaleimide
C430A
ABA3-NifS, reduced activity to 14% for L-cysteine and 20% for L-selenocysteine
C435A
the mutant is less sensitive towards N-ethylmaleimide compared to the wild type enzyme
R723K
C-terminal domain of ABA3, reduced molybdenum cofactor binding
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-nitrilotriacetic acid superflow matrix, UNO Q-1 column, Superose 12 size exclusion column
nickel-nitrilotriacetic acid superflow matrix, UNO Q-1 column, Superose 12 size exclusion column
nickel-nitrilotriacetic acid superflow matrix, UNO Q-1 column, Superose 12 size exclusion column
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum leaves using Agrobacterium-mediated transformation
-
in vector pQE80
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ABA3 mRNA levels rapidly increase within 3 h of treatment with polyethylene glycol and are sustained for 24 h
the enzyme expression is induced by heat (45°C), dehydration, high salt stresses (200 mM NaCl), and abscisic acid (0.008 mM) induction
the enzyme expression is inhibited by cold stress (4°C and -12°C)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
overexpression in Sesamum indicum. Under severe drought conditions, transgenic plants show less reduction in height compared to azygous non-transgenic plants. Increase in total extractable soluble proteins, elevation in proline accumulation, and a reduction in MDA levels are recorded in transgenic lines. Under non-stressed conditions, ascorbate peroxidase, catalase, peroxidase and superoxide dismutase activity levels increase by 25%, 23%, 210% and 75%, respectively, compared to azygous non-transgenic plants
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bittner, F.; Oreb, M.; Mendel, R.R.
ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana
J. Biol. Chem.
276
40381-40384
2001
Arabidopsis thaliana (Q9C5X8), Arabidopsis thaliana
brenda
Heidenreich, T.; Wollers, S.; Mendel, R.R.; Bittner, F.
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration
J. Biol. Chem.
280
4213-4218
2005
Arabidopsis thaliana (Q9C5X8), Arabidopsis thaliana
brenda
Wollers, S.; Heidenreich, T.; Zarepour, M.; Zachmann, D.; Kraft, C.; Zhao, Y.; Mendel, R.R.; Bittner, F.
Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration
J. Biol. Chem.
283
9642-9650
2008
Arabidopsis thaliana (Q9C5X8), Arabidopsis thaliana
brenda
Lehrke, M.; Rump, S.; Heidenreich, T.; Wissing, J.; Mendel, R.R.; Bittner, F.
Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis
Biochem. J.
441
823-832
2012
Arabidopsis thaliana (Q9C5X8), Arabidopsis thaliana
brenda
Li, Y.; Zhang, J.; Zhang, J.; Hao, L.; Hua, J.; Duan, L.; Zhang, M.; Li, Z.
Expression of an Arabidopsis molybdenum cofactor sulphurase gene in soybean enhances drought tolerance and increases yield under field conditions
Plant Biotechnol. J.
11
747-758
2013
Arabidopsis thaliana
brenda
Yue, Y.; Zhang, M.; Zhang, J.; Duan, L.; Li, Z.
Arabidopsis LOS5/ABA3 overexpression in transgenic tobacco (Nicotiana tabacum cv. Xanthi-nc) results in enhanced drought tolerance
Plant Sci.
181
405-411
2011
Arabidopsis thaliana
brenda
Lu, Y.; Li, Y.; Zhang, J.; Xiao, Y.; Yue, Y.; Duan, L.; Zhang, M.; Li, Z.
Overexpression of Arabidopsis molybdenum cofactor sulfurase gene confers drought tolerance in maize (Zea mays L.)
PLoS ONE
8
e52126
2013
Arabidopsis thaliana
brenda
Yu, H.Q.; Zhang, Y.Y.; Yong, T.M.; Liu, Y.P.; Zhou, S.F.; Fu, F.L.; Li, W.C.
Cloning and functional validation of molybdenum cofactor sulfurase gene from Ammopiptanthus nanus
Plant Cell Rep.
34
1165-1176
2015
Ammopiptanthus nanus (A0A0B5A169), Ammopiptanthus nanus
brenda
Al-Shafeay, A.; Ibrahim, A.; Nesiem, M.; Tawfik, M.
Dehydration stress tolerance in sesame plants (Sesamum indicum L.) over expressing the Arabidopsis thaliana molybdenum cofactor sulfurase LOS5/aba3 gene under greenhouse conditions
Biosci. Res.
15
3131-3143
2018
Arabidopsis thaliana (Q9C5X8)
-
brenda
Watanabe, S.; Sato, M.; Sawada, Y.; Tanaka, M.; Matsui, A.; Kanno, Y.; Hirai, M.Y.; Seki, M.; Sakamoto, A.; Seo, M.
Arabidopsis molybdenum cofactor sulfurase ABA3 contributes to anthocyanin accumulation and oxidative stress tolerance in ABA-dependent and independent ways
Sci. Rep.
8
16592
2018
Arabidopsis thaliana (Q9C5X8)
brenda
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