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Information on EC 1.1.1.216 - farnesol dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.216
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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
1.1.1.216 farnesol dehydrogenase (NADP+)
IUBMB Comments
Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol.
The enzyme appears in viruses and cellular organisms
showSynonyms
sdr-1, nad(p)+-dependent farnesol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, farnesol (nicotinamide adenine dinucleotide phosphate)
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NADP-farnesol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesol + NADP+ = (2E,6E)-farnesal + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
farnesylcysteine salvage pathway, juvenile hormone III biosynthesis I, juvenile hormone III biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesol:NADP+ 1-oxidoreductase
Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol.
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CAS REGISTRY NUMBER
COMMENTARY
90804-55-0
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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
(2E,6E)-farnesol + NAD+
(2E,6E)-farnesal + NADH + H+
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Substrates: preferred substrates
Products: -
Products: -
?
(2Z,6E)-farnesol + NAD+
(2Z,6E)-farnesal + NADH + H+
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Substrates: 66% of the activity with 2-trans,6-trans-farnesol
Products: -
Products: -
?
(2Z,6Z)-farnesol + NAD+
(2Z,6Z)-farnesal + NADH + H+
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Substrates: 47% of the activity with 2-trans,6-trans-farnesol
Products: -
Products: -
?
(2Z,6Z)-farnesol + NADP+
(2Z,6Z)-farnesal + NADPH + H+
Substrates: enzyme shows highest affinity for farnesol
Products: -
Products: -
r
(E)-geraniol + NADP+
(E)-geranial + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-perillyl alcohol + NAD+
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Substrates: 34% of the activity with 2-trans,6-trans-farnesol
Products: -
Products: -
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carveol + NAD+
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Substrates: 32% of the activity with 2-trans,6-trans-farnesol
Products: -
Products: -
?
cinnamyl alcohol + NAD+
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Substrates: 35% of the activity with 2-trans,6-trans-farnesol
Products: -
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?
cis,trans-farnesol + NADP+
cis,trans-farnesal + NADPH
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Substrates: -
Products: -
Products: -
?
citronellol + NADP+
citronellal + NADPH + H+
Substrates: -
Products: -
Products: -
?
geraniol + NAD+
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Substrates: 37% of the activity with 2-trans,6-trans-farnesol
Products: -
Products: -
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nerodilol + NAD+
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Substrates: 36% of the activity with 2-trans,6-trans-farnesol
Products: -
Products: -
?
trans,trans-farnesol + NADP+
trans,trans-farnesal + NADPH
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Substrates: preferred substrate
Products: -
Products: -
r
(2E,6E)-farnesol + NADP+
(2E,6E)-farnesal + NADPH + H+
Substrates: enzyme shows highest affinity for farnesol
Products: -
Products: -
ir
(2E,6E)-farnesol + NADP+
(2E,6E)-farnesal + NADPH + H+
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Substrates: NADP+ show 22% of the activity with NAD+
Products: -
Products: -
?
(2E,6E)-farnesol + NADP+
(2E,6E)-farnesal + NADPH + H+
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Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesol + NADP+
(2E,6E)-farnesal + NADPH + H+
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Substrates: -
Products: -
Products: -
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additional information
?
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Substrates: no activity is detected for butanol, ethanol, or glycerol, or for farnesal or farnesoic acid
Products: -
Products: -
?
additional information
?
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Substrates: trans,trans-farnesol is the preferred substrate for the Polygonum minus farnesol dehydrogenase, the geometrical isomers cis,trans-farnesol and cis,cis-farnesol are also oxidized by the enzyme with lower activity. No activity with nerol, p-cumic alcohol, borneol, linalool, menthol, beta-citronellol, 3,7-dihydrolinalool, benzyl alcohol, 2,4-octadien-1-ol, or 2,5-dimethyl-1.5-hexadien-3-ol, tetrahydrogeraniol, tetrahydrolinalool, tetrahydrolavandulol, ethanol, and methanol. Substrate specificity, overview
Products: -
Products: -
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additional information
?
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Substrates: enzyme is highly specific for trans, trans-farnesol, and NADP+
Products: -
Products: -
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additional information
?
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Substrates: (2E,6E)-farnesol is the most preferred substrate
Products: -
Products: -
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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the enzyme utilizes both NAD+ and NADP+ with a strong preference for NAD+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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inhibitory effect of thiol reagents indicates that the SH-group of the enzyme participates in its activity
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additional information
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the enzyme activity is inhibited by sulfhydryl reagents, metal-chelating agents and heavy metal ions
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
farnesyl acetate
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pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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reduction of trans,trans-farnesal: 60% of maximal activity at pH 6.5 and at pH 8
7 - 10.5
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oxidation of trans,trans-farnesol: 10% of maximal activity at pH 7.0, 30% of maximal activity at pH 10.2
7.5 - 11
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activity range, profile overview. At below pH 8.5 or above pH 10.0, the enzyme activity declines sharply
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
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
sweet potato, enzyme is formed in response to infection by the black rot fungus Ceratocystis fimbriata
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brenda
plants growing in an experimental plot at the Institute of Systems Biology of Universiti Kebangsaan Malaysia
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
no farnesol dehydrogenase activity in newly emerged mosquitoes but significant activity 24 h later. SDR-1 mRNA levels are very low in the inactive corpora allata of the newly emerged female, but increased over 30-fold 24 h later during the peak of juvenile hormone synthesis
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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the enzyme is involved in the biosynthesis of precursors that can be used for the biosynthetic pathway of juvenile hormone III (JH III, methyl-10R,11-epoxy-3,7,11-trimethyl-2E,6E-dodecadienoate). Deployment of transgenic plant with farnesol dehydrogenase enzyme will be beneficial for use in manipulating juvenile hormone biosynthesis in plants
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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
dimer
additional information
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tryptic peptide mapping and MALDI-TOF/TOF-MS spectrometric analysis, sequence comparisons, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 65
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purified native enzyme, 10 min at pH 7.5 in 100 mM tricine-NaOH containing 2.5 mM 2-mercaptoethanol, completely stable up to 30°C, over 90% activity up to 55°C, loss of 80% activity at 60°C, loss of 85% activity at 65°C, and inactivation at 70°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 234fold from leaves to apparent homogeneity by two different steps of anion-exchange chromatography and a cation exchange chromatography step, followed by three successive steps of gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SDR-1 mRNA levels are very low in the inactive corpora allata of the newly emerged female, but increased over 30-fold 24 h later during the peak of juvenile hormone synthesis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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recombinant farnesol dehydrogenase may provide a useful molecular tool in manipulating juvenile hormone biosynthesis to generate transgenic plants for pest control
biotechnology
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recombinant farnesol dehydrogenase may provide a useful molecular tool in manipulating juvenile hormone biosynthesis to generate transgenic plants for pest control
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Inoue, H.; Tsuji, H.; Uritani, I.
Characteriziation and activity change of farnesol dehydrogenase in black rot fungus-infected sweet potato
Agric. Biol. Chem.
48
733-738
1984
Ipomoea batatas
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brenda
Sperry, A.E.; Sen, S.E.
Farnesol oxidation in insects: evidence that the biosynthesis of insect juvenile hormone is mediated by a specific alcohol oxidase
Insect Biochem. Mol. Biol.
31
171-178
2001
Manduca sexta
brenda
Mayoral, J.G.; Nouzova, M.; Navare, A.; Noriega, F.G.
NADP+-dependent farnesol dehydrogenase, a corpora allata enzyme involved in juvenile hormone synthesis
Proc. Natl. Acad. Sci. USA
106
21091-21096
2009
Aedes aegypti (D2WKD9)
brenda
Ahmad-Sohdi, N.A.; Seman-Kamarulzaman, A.F.; Mohamed-Hussein, Z.A.; Hassan, M.
Purification and characterization of a novel NAD(P)+-farnesol dehydrogenase from Polygonum minus leaves
PLoS ONE
10
e0143310
2015
Persicaria minor
brenda
Zifruddin, A.N.; Mohamad-Khalid, K.A.; Suhaimi, S.A.; Mohamed-Hussein, Z.A.; Hassan, M.
Molecular characterization and enzyme inhibition studies of NADP+-farnesol dehydrogenase from diamondback moth, Plutella xylostella (Lepidoptera Plutellidae)
Biosci. Biotechnol. Biochem.
85
1628-1638
2021
Plutella xylostella
brenda
Satyaveanthan, M.; Suhaimi, S.; Ng, C.; Muhd-Noor, N.; Awang, A.; Lam, K.; Hassan, M.
Purification, biochemical characterisation and bioinformatic analysis of recombinant farnesol dehydrogenase from Theobroma cacao
Plant Physiol. Biochem.
161
143-155
2021
Theobroma cacao
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.216)
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