Information on EC 4.2.1.94 - scytalone dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.94
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RECOMMENDED NAME
GeneOntology No.
scytalone dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
scytalone = 1,3,8-trihydroxynaphthalene + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
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-
-
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SYSTEMATIC NAME
IUBMB Comments
scytalone 7,8-hydro-lyase (1,3,8-trihydroxynaphthalene-forming)
Involved, with EC 1.1.1.252 tetrahydroxynaphthalene reductase, in the biosynthesis of melanin in pathogenic fungi.
CAS REGISTRY NUMBER
COMMENTARY hide
118901-79-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
gene sal1
UniProt
Manually annotated by BRENDA team
gene sal1
UniProt
Manually annotated by BRENDA team
no activity in yeast extracts that do not form pentaketide melanins
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-
-
Manually annotated by BRENDA team
Phaeococcomyces sp.
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-
-
Manually annotated by BRENDA team
not in extracts from organisms that had not yet formed melanin
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-
Manually annotated by BRENDA team
not in extracts from organisms that had not yet formed melanin
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one
5-hydroxy-4H-benzopyran-4-one + H2O
show the reaction diagram
deshydroxyvermelone
1-naphthol + H2O
show the reaction diagram
-
-
-
r
scytalone
1,3,8-trihydroxynaphthalene + H2O
show the reaction diagram
vermelone
1,8-dihydroxynaphthalene + H2O
show the reaction diagram
additional information
?
-
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
scytalone
1,3,8-trihydroxynaphthalene + H2O
show the reaction diagram
additional information
?
-
-
among 1175 isolates collected from 6 prefectures of Kyushu in 2002 and 2003, 647 are resistant to MBI-D fungicides (inhibitors of melanin biosynthesis), each due to a single point mutation of the scytalone dehydratase gene. Isolates possessing the mutation in the scytalone dehydratase gene would have been selected and then multiplied rapidly in each region of Kyushu as a result of the wide-spread introduction of MBI-D fungicides in a short period
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1RS,3RS)-2,2-dichloro-N-[(R)-1-(4-chlorophenyl)ethyl]-1-ethyl-3-methylcyclopropanecarboxamide
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i.e. carpropamid
1,2,5,6-Tetrahydro-4H-pyrrolo[3,2,1-i,j]quinolin-4-one
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i.e. pyroquilon
2,3,4,5,6-Pentachlorobenzyl alcohol
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-
4,5,6,7-Tetrachorophthalide
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i.e. fthalide
4,5-Dihydro-4-methyltetrazolo-[1,5-a]-quinazolin-5-one
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4-Chloro-3-methylbenzothiazol-2[3H]-one
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i.e. chlorobenthiazone
5-Methyl-1,2,4-triazolo[3,4-b]-benzothiazole
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i.e. tricyclazole
aminoquinazoline
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-
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carpropamide
i.e. (1RS,3SR)-2,2-dichloro-N-[(R)-1-(4-chlorophenyl)ethyl]-1-ethyl-3-methylcyclopropanecarboxamide
coumarin
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-
KTU3615A
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competitive
KTU3615B
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competitive
KTU3616A
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competitive
KTU3616B
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competitive
N-Methyl-2-quinolone
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s-Triazolo[4,3-a]-quinoline
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-
additional information
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inhibitors that display variations in the hydrophilic region of the SD binding site, kinetic data for wild type and mutant enzymes
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
2,3-Dihydro-2,5-dihydroxy-4H-benzopyran-4-one
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25C, pH 7.0
0.021 - 33
Scytalone
31
Vermelone
-
25C, pH 7.0
additional information
additional information
-
Km values and kinetic konstants of several mutants
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 70
Scytalone
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000024
KTU3615A
-
pH 7.0, 30C, wild-type enzme
0.000011
KTU3616A
-
pH 7.0, 30C, wild-type enzme
0.0000001
KTU3616B
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pH 7.0, 30C, wild-type enzme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36.6
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30C, pH 8.2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
Phaeococcomyces sp.
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maximal activity under anaerobic conditions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
Phaeococcomyces sp.
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pH 6.5: about 65% of maximum activity, pH 8: about 60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
x * 23000, SDS-PAGE
58000 - 60000
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ultracentrifugation studies
63000
Phaeococcomyces sp.
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PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
enzyme is present in solution as a trimer, ultracentrifugation studies, crystallographic data
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
Phaeococcomyces sp.
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with an aminoquinazoline inhibitor
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in complex with the tight binding inhibitor carpropamid
mutant F162A
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 3 months
Phaeococcomyces sp.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Phaeococcomyces sp.
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in the amelanotic entomopathogenic fungus Metarhizium anisopliae via Agrobacterium-mediated transformation. The transformant, especially under stresses, shows notably enhanced antistress capacity and virulence, in terms of germination and survival rate, infectivity, and reduced median time to death in killing diamondback moth, Plutella xylostella, larvae compared with the wild-type
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gene CmSCD1, DNA and amino acid sequence determination and analysis, quantitative Taqman real-time PCR expression analysis and comparative analysis of the nucleotide sequences of CmSCD1 from Korean strains with those from the Japanese and Taiwanese strains
gene sal1, DNA and amino acid sequence determination and analysis
overexpression of V75M in Escherichia coli with or without an N-terminal histidine-tag
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F162A
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crystal structure
V75M
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inhibition of the mutant enzyme by (1RS,3RS)-2,2-dichloro-N-[(R)-1-(4-chlorophenyl)ethyl]-1-ethyl-3-methylcyclopropanecarboxamide is more than 200fold reduced in comparison with that of the wild-type, about 2fold reduced turnover number for scytalone as compared to wild-type enzyme
additional information
Show AA Sequence (226 entries)
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