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Enzyme Nomenclature
Information on EC 2.8.1.9 - molybdenum cofactor sulfurtransferase
for references in articles please use BRENDA:EC2.8.1.9
Word Map on EC 2.8.1.9
- 2.8.1.9
- aldehyde
-
abscisic
- mocos
-
drought
-
xanthinuria
-
nifs-like
-
desulfurase
-
transpirational
- persulfide
-
wilting
-
amidoxime
- allopurinol
-
two-domain
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.8.1.9
-
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RECOMMENDED NAME
GeneOntology No.
molybdenum cofactor sulfurtransferase
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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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
-
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
-
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 enhances the tolerance to high salt, cold, osmotic stresses, and abscisic acid induction
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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
-
-
-
?
additional information
?
-
-
no detectable activity for L-cysteine ethylester, glutathione, beta-mercaptopyruvate, L-cysteamine, and L-cystine
-
-
-
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
-
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
A0A0B5A169
-
-
-
?
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
Q9C5X8
-
-
-
?
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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INHIBITORS
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
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
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LINKS TO OTHER DATABASES (specific for EC-Number 2.8.1.9)
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