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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 + H+
thio-molybdenum cofactor + L-alanine + H2O
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
-
-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
additional information
?
-
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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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
-
-
-
?
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
-
-
-
-
?
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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metabolism
molybdenum cofactor biosynthesis
metabolism
-
molybdenum cofactor biosynthesis
metabolism
molybdenum cofactor biosynthesis
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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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