BRENDA - Enzyme Database show
show all sequences of 4.2.3.104

Characterization of alpha-humulene synthases responsible for the production of sesquiterpenes induced by methyl jasmonate in Aquilaria cell culture

Kumeta, Y.; Ito, M.; J. Nat. Med. 70, 452-459 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene HS1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, heterologous expression of the enzyme in Escherichia coli; gene HS2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, heterologous expression of the enzyme in Escherichia coli; gene HS3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, heterologous expression of the enzyme in Escherichia coli
Aquilaria crassna
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
the enzyme has no N-terminal transit peptide; the enzyme has no N-terminal transit peptide; the enzyme has no N-terminal transit peptide
Aquilaria crassna
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2E,6E)-farnesyl diphosphate
Aquilaria crassna
-
alpha-humulene + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aquilaria crassna
A0A142F308
-
-
Aquilaria crassna
A0A142F309
-
-
Aquilaria crassna
A0A142F310
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
additional information
the enzyme has no N-terminal transit peptide; the enzyme has no N-terminal transit peptide; the enzyme has no N-terminal transit peptide
Aquilaria crassna
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2E,6E)-farnesyl diphosphate
-
748440
Aquilaria crassna
alpha-humulene + diphosphate
-
-
-
?
additional information
the recombinant alpha-humulene synthase isozyme HS1 produces 94.6% alpha-humulene and 5.4% beta-caryophyllene
748440
Aquilaria crassna
?
-
-
-
-
additional information
the recombinant alpha-humulene synthase isozyme HS2 produces 95.0% alpha-humulene and 5.0% beta-caryophyllene
748440
Aquilaria crassna
?
-
-
-
-
additional information
the recombinant alpha-humulene synthase isozyme HS3 produces 93.5% alpha-humulene and 6.5% beta-caryophyllene
748440
Aquilaria crassna
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
gene HS1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, heterologous expression of the enzyme in Escherichia coli
Aquilaria crassna
gene HS2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, heterologous expression of the enzyme in Escherichia coli
Aquilaria crassna
gene HS3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, heterologous expression of the enzyme in Escherichia coli
Aquilaria crassna
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
the enzyme has no N-terminal transit peptide
Aquilaria crassna
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2E,6E)-farnesyl diphosphate
Aquilaria crassna
-
alpha-humulene + diphosphate
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
additional information
the enzyme has no N-terminal transit peptide
Aquilaria crassna
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2E,6E)-farnesyl diphosphate
-
748440
Aquilaria crassna
alpha-humulene + diphosphate
-
-
-
?
additional information
the recombinant alpha-humulene synthase isozyme HS1 produces 94.6% alpha-humulene and 5.4% beta-caryophyllene
748440
Aquilaria crassna
?
-
-
-
-
additional information
the recombinant alpha-humulene synthase isozyme HS2 produces 95.0% alpha-humulene and 5.0% beta-caryophyllene
748440
Aquilaria crassna
?
-
-
-
-
additional information
the recombinant alpha-humulene synthase isozyme HS3 produces 93.5% alpha-humulene and 6.5% beta-caryophyllene
748440
Aquilaria crassna
?
-
-
-
-
Expression
Organism
Commentary
Expression
Aquilaria crassna
methyl jasmonate slightly induces the expression of enzyme alpha-humulene synthase, at 6 h after methyl jasmonate treatment, the expression of the alpha-humulene synthase gene has increased approximately 1.5fold resulting in 330 pmol/mg protein/h alpha-humulene production; methyl jasmonate slightly induces the expression of enzyme alpha-humulene synthase, at 6 h after methyl jasmonate treatment, the expression of the alpha-humulene synthase gene has increased approximately 1.5fold resulting in 330 pmol/mg protein/h alpha-humulene production; methyl jasmonate slightly induces the expression of enzyme alpha-humulene synthase, at 6 h after methyl jasmonate treatment, the expression of the alpha-humulene synthase gene has increased approximately 1.5fold resulting in 330 pmol/mg protein/h alpha-humulene production
up
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in the biosynthetic pathways for sesquiterpenes found in agarwood and cell suspension cultures, putative pathway, overview. Various post-transcriptional, translational, or post-translational regulatory mechanisms affecting the expression or activity of alpha-humulene and delta-guaiene synthases are possible; the enzyme is involved in the biosynthetic pathways for sesquiterpenes found in agarwood and cell suspension cultures, putative pathway, overview. Various post-transcriptional, translational, or post-translational regulatory mechanisms affecting the expression or activity of alpha-humulene and delta-guaiene synthases are possible; the enzyme is involved in the biosynthetic pathways for sesquiterpenes found in agarwood and cell suspension cultures, putative pathway, overview. Various post-transcriptional, translational, or post-translational regulatory mechanisms affecting the expression or activity of alpha-humulene and delta-guaiene synthases are possible
Aquilaria crassna
additional information
the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site; the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site; the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site
Aquilaria crassna
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in the biosynthetic pathways for sesquiterpenes found in agarwood and cell suspension cultures, putative pathway, overview. Various post-transcriptional, translational, or post-translational regulatory mechanisms affecting the expression or activity of alpha-humulene and delta-guaiene synthases are possible
Aquilaria crassna
additional information
the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site
Aquilaria crassna
Expression (protein specific)
Organism
Commentary
Expression
Aquilaria crassna
methyl jasmonate slightly induces the expression of enzyme alpha-humulene synthase, at 6 h after methyl jasmonate treatment, the expression of the alpha-humulene synthase gene has increased approximately 1.5fold resulting in 330 pmol/mg protein/h alpha-humulene production
up
Other publictions for EC 4.2.3.104
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746751
Krieg
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Cupriavidus necator
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57
1879-1882
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748561
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Production of sesquiterpenoid ...
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1
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1
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1
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1
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747656
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4
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1
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3
1
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1
1
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746789
Alemdar
Heterologous expression, puri ...
Zingiber zerumbet
Appl. Biochem. Biotechnol.
178
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1
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1
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2
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1
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1
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1
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1
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2
1
1
1
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1
1
1
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2
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2
2
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748440
Kumeta
Characterization of alpha-hum ...
Aquilaria crassna
J. Nat. Med.
70
452-459
2016
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1
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1
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3
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3
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1
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6
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6
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1
2
6
3
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748552
Sonntag
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Zingiber zerumbet
Metab. Eng.
32
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1
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1
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730575
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Gossypium hirsutum
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1
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5
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7
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2
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1
1
1
2
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716562
Bleeker
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Solanum habrochaites
Plant Mol. Biol.
77
323-336
2011
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1
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717468
Yu
Zingiber zerumbet CYP71BA1 cat ...
Zingiber zerumbet
Cell. Mol. Life Sci.
68
1033-1040
2011
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1
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1
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1
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716459
Koepke
Species-specific responses of ...
Pinus sylvestris
Phytochemistry
71
909-917
2010
-
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8
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1
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1
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718233
Schilmiller
Studies of a biochemical facto ...
Solanum lycopersicum
Plant Physiol.
153
1212-1223
2010
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1
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690593
Harada
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Zingiber zerumbet
Appl. Microbiol. Biotechnol.
81
915-925
2008
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1
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6
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1
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1
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1
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718244
Yu
Molecular cloning and function ...
Zingiber zerumbet
Planta
227
1291-1299
2008
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1
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3
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1
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1
1
1
1
1
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713266
van Der Hoeven
Genetic control and evolution ...
no activity in Solanum habrochaites, Solanum lycopersicum
Plant Cell
12
2283-2294
2000
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