Information on EC 2.8.1.9 - molybdenum cofactor sulfurtransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.1.9
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RECOMMENDED NAME
GeneOntology No.
molybdenum cofactor sulfurtransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
thio-molybdenum cofactor biosynthesis
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molybdenum cofactor biosynthesis
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Folate biosynthesis
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cysteine
L-alanine + H2S
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
show the reaction diagram
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-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
show the reaction diagram
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
molybdenum cofactor + L-cysteine + H+
thio-molybdenum cofactor + L-alanine + H2O
show the reaction diagram
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+
thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
show the reaction diagram
A0A0B5A169
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-
-
?
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+
MoOS(OH)Dtpp-mP + L-alanine + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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highest levels in leaves and roots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92600
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calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 84850, calculated from amino acid sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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in vector pQE80
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C101/C430A
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inactive
C151/C430A
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inactive
C206S
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the mutant‘s activity is reduced to 18%
C206S/C430A
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inactive
C250/C430A
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inactive
C377/C430A
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inactive
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
C456/C430A
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inactive
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
Show AA Sequence (807 entries)
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