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Enzyme Nomenclature
Information on EC 1.1.1.326 - zerumbone synthase
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The expected taxonomic range for this enzyme is: Zingiber zerumbet
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EC NUMBER 
COMMENTARY 
1.1.1.326
-
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RECOMMENDED NAME
GeneOntology No.
zerumbone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10-hydroxy-alpha-humulene + NAD+ = zerumbone + NADH + H+
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
10-hydroxy-?-humulene:NAD+ oxidoreductase
The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
ZSD1 is a member of the short-chain dehydrogenase/reductase superfamily, SDR, and shares high identities with other plant SDRs involved in secondary metabolism, stress responses and phytosteroid biosynthesis
metabolism
ZSD1 is an alcohol dehydrogenase capable of catalyzing the final step of zerumbone biosynthesis, but ZSD1 is also be involved in other biological processes
physiological function
ZSD1 is involved in secondary metabolism, stress responses and phytosteroid biosynthesis
additional information
the enzyme contains an active site sequence 155Y-X-X-X-K159, Ser142 completes the Ser-Tyr-Lys triad responsible for the catalysis of ZSD1
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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
additional information
?
-
the enzyme also converts borneol to camphor in vitro with Km and kcat values of 0.0228 mM and 4.1/s
-
-
-
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
the enzyme possesses a flexible substrate-binding pocket and converts 10-hydroxy-alpha-humulene into zerumbone
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-
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics with borneol as substrate
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0.028
10-hydroxy-alpha-humulene
recombinant mutant S144A, pH 8.0, 37°C
0.0585
10-hydroxy-alpha-humulene
recombinant wild-type enzyme, pH 8.0, 37°C
0.0782
10-hydroxy-alpha-humulene
recombinant mutant Y155A, pH 8.0, 37°C
0.138
10-hydroxy-alpha-humulene
recombinant mutant S142A, pH 8.0, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant mutant S142A, pH 8.0, 37°C; recombinant mutant Y155A, pH 8.0, 37°C
1.3
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant wild-type enzyme, pH 8.0, 37°C
2.9
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant mutant S144A, pH 8.0, 37°C
0.1
NAD+
Zingiber zerumbet
F1SWA0
recombinant mutant S142A, pH 8.0, 37°C; recombinant mutant Y155A, pH 8.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000007
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant mutant S142A, pH 8.0, 37°C
6389
0.000001
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant mutant Y155A, pH 8.0, 37°C
6389
0.000022
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant wild-type enzyme, pH 8.0, 37°C
6389
0.000103
10-hydroxy-alpha-humulene
Zingiber zerumbet
F1SWA0
recombinant mutant S144A, pH 8.0, 37°C
6389
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
contains an exceptionally high level of sesquiterpenoids with zerumbone
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a 3D structure model of ZSD1 reveals a large, flexible substrate-binding pocket, molecular modeling, overview
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ZSD1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S142A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S144A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y155A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
zerumbone is a predominating potential multi-anticancer agent
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.326)
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