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Information on EC 1.1.1.326 - zerumbone synthase
for references in articles please use BRENDA:EC1.1.1.326
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.326 zerumbone synthase
IUBMB Comments
The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
The expected taxonomic range for this enzyme is: Zingiber zerumbet
showSynonyms
zerumbone synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10-hydroxy-alpha-humulene + NAD+ = zerumbone + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
zerumbone biosynthesis
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: the enzyme also converts borneol to camphor in vitro with Km and kcat values of 0.0228 mM and 4.1/s
Products: -
Products: -
?
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
Substrates: -
Products: -
Products: -
?
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
Substrates: the enzyme possesses a flexible substrate-binding pocket and converts 10-hydroxy-alpha-humulene into zerumbone
Products: -
Products: -
?
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
Substrates: -
Products: -
Products: -
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
Substrates: -
Products: -
Products: -
?
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
Substrates: -
Products: -
Products: -
r
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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
-
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
recombinant mutant Y155A, pH 8.0, 37°C
0.1
10-hydroxy-alpha-humulene
recombinant mutant S142A, pH 8.0, 37°C
1.3
10-hydroxy-alpha-humulene
recombinant wild-type enzyme, pH 8.0, 37°C
2.9
10-hydroxy-alpha-humulene
recombinant mutant S144A, 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
recombinant mutant S142A, pH 8.0, 37°C
0.000001
10-hydroxy-alpha-humulene
recombinant mutant Y155A, pH 8.0, 37°C
0.000022
10-hydroxy-alpha-humulene
recombinant wild-type enzyme, pH 8.0, 37°C
0.000103
10-hydroxy-alpha-humulene
recombinant mutant S144A, pH 8.0, 37°C
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
contains an exceptionally high level of sesquiterpenoids with zerumbone
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
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
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
evolution
the enzyme belongs to the short-chain dehydrogenase enzyme superfamily
physiological function
ZSD1 is involved in secondary metabolism, stress responses and phytosteroid biosynthesis
physiological function
the enzyme catalyzes the biosynthesis of zerumbone, a monocyclic sesquiterpenoid ketone with potential anti-inflammatory and anti-carcinogenic effects and also potential applications in obesity prevention and treatment
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S114A
site-directed mutagenesis, the mutation of Ser144 to Ala enhances the catalytic efficiency of ZSD1 to 10-hydroxy-alpha-humulene compared to wild-type
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
additional information
additional information
de novo production of zerumbone is achieved in a metabolically engineered yeast cell factory by introducing alpha-humulene synthase (ZSS1), alpha-humulene 8-hydroxylase (CYP71BA1), and zerumbone synthase variant (ZSD1S114A) from Zingiber zerumbet, together with AtCPR1 from Arabidopsis thaliana into a Saccharomyces cerevisiae strain LW14-16. The overexpression of the mevalonate (MVA) pathway rate-limiting enzymes tHMG1 and ERG20, regulation of ERG9 by an inducible promoter and competitive pathway deletion redirects the metabolic flux toward the desired product. Expressing ZSD1S114A in the ura3 site of strain LW14 results in the production of 7 mg/l zerumbone, multicopy integration of ZSD1S114A increases the production of zerumbone to 20.6 mg/l, production of zerumbone finally reached 40 mg/l by fed-batch fermentation in a 5-l bioreactor using strain LW16, method overview
additional information
-
de novo production of zerumbone is achieved in a metabolically engineered yeast cell factory by introducing alpha-humulene synthase (ZSS1), alpha-humulene 8-hydroxylase (CYP71BA1), and zerumbone synthase variant (ZSD1S114A) from Zingiber zerumbet, together with AtCPR1 from Arabidopsis thaliana into a Saccharomyces cerevisiae strain LW14-16. The overexpression of the mevalonate (MVA) pathway rate-limiting enzymes tHMG1 and ERG20, regulation of ERG9 by an inducible promoter and competitive pathway deletion redirects the metabolic flux toward the desired product. Expressing ZSD1S114A in the ura3 site of strain LW14 results in the production of 7 mg/l zerumbone, multicopy integration of ZSD1S114A increases the production of zerumbone to 20.6 mg/l, production of zerumbone finally reached 40 mg/l by fed-batch fermentation in a 5-l bioreactor using strain LW16, method 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)
gene zsd1, recombinant expression in Saccharomyces cerevisiae strain W303-1a, functional co-expression with alpha-humulene synthase (ZSS1), alpha-humulene 8-hydroxylase (CYP71BA1), and AtCPR1 from Arabidopsis thaliana, subcloning in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
zerumbone is a predominating potential multi-anticancer agent
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okamoto, S.; Yu, F.; Harada, H.; Okajima, T.; Hattan, J.; Misawa, N.; Utsumi, R.
A short-chain dehydrogenase involved in terpene metabolism from Zingiber zerumbet
FEBS J.
278
2892-2900
2011
Zingiber zerumbet (F1SWA0)
brenda
Zhang, C.; Liu, J.; Zhao, F.; Lu, C.; Zhao, G.R.; Lu, W.
Production of sesquiterpenoid zerumbone from metabolic engineered Saccharomyces cerevisiae
Metab. Eng.
49
28-35
2018
Zingiber zerumbet (F1SWA0), Zingiber zerumbet
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.326)
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Release 2026.1 (March 2026)
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