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Information on EC 2.8.1.9 - molybdenum cofactor sulfurtransferase for references in articles please use BRENDA:EC2.8.1.9Word Map on EC 2.8.1.9
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The enzyme appears in viruses and cellular organisms
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molybdenum cofactor sulfurtransferase
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molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
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thio-molybdenum cofactor biosynthesis
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molybdenum cofactor biosynthesis
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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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molybdenum cofactor sulfurase
molybdenum cofactor sulphurase
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molybdenum-cofactor sulfurase
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ABA3
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molybdenum cofactor sulfurase
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molybdenum cofactor sulfurase
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UniProt
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SwissProt
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metabolism
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molybdenum cofactor biosynthesis
metabolism
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molybdenum-cofactor sulfurase is a key regulator of abscisic acid biosynthesis
physiological function
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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
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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
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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 enhances the tolerance to high salt, cold, osmotic stresses, and abscisic acid induction
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L-cysteine
L-alanine + H2S
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in presence of DTT as reducing agent, activity of the the cysteine desulfurase domain
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L-cysteine methyl ester
L-alanine methyl ester + H2S
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in presence of DTT as reducing agent, activity of the the cysteine desulfurase domain
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L-selenocysteine
L-alanine + H2Se
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in presence of DTT as reducing agent, activity of the the cysteine desulfurase domain
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molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
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MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
additional information
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no detectable activity for L-cysteine ethylester, glutathione, beta-mercaptopyruvate, L-cysteamine, and L-cystine
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molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
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molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
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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
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MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
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MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
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molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
A0A0B5A169
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MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
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molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
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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
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MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
Q9C5X8
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MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
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pyridoxal 5'-phosphate
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N-ethylmaleimide
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4fold excess, 71% inhibition
N-ethylmaleimide
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less than 80% activity at 1 mM, 30% activity at 1.5 mM, complete inhibition at 2 mM
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0.05
L-cysteine
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for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
0.2
L-selenocysteine
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for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
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0.03
L-cysteine
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for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
0.357
L-selenocysteine
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for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C
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highest levels in leaves and roots
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highest levels in leaves and roots
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92600
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calculated from sequence
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x * 84850, calculated from amino acid sequence
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Ni-NTA column chromatography
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nickel-nitrilotriacetic acid superflow matrix, UNO Q-1 column, Superose 12 size exclusion column
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expressed in Escherichia coli DL41 cells
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expressed in Glycine max leaves
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expressed in Nicotiana benthamiana and Arabidopsis thaliana
expressed in Nicotiana tabacum leaves using Agrobacterium-mediated transformation
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expressed in Zea mays leaves
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enzyme expression is up-regulated by drought stress
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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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C206S
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the mutant‘s activity is reduced to 18%
C428/435A
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the mutant shows wild type sensitivity towards N-ethylmaleimide
C430A
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ABA3-NifS, reduced activity to 14% for L-cysteine and 20% for L-selenocysteine
C435A
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the mutant is less sensitive towards N-ethylmaleimide compared to the wild type enzyme
K271S
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ABA3-NifS, inactive, unable to bind pyridoxal 5'-phosphate
R723K
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C-terminal domain of ABA3, reduced molybdenum cofactor binding
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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, Arabidopsis thaliana (Q9C5X8)
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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, Arabidopsis thaliana (Q9C5X8)
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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, Arabidopsis thaliana (Q9C5X8)
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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, Arabidopsis thaliana (Q9C5X8)
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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
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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
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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
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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
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