Any feedback?
No. of entries
Information on EC 2.5.1.70 - naringenin 8-dimethylallyltransferase
for references in articles please use BRENDA:EC2.5.1.70
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.70 naringenin 8-dimethylallyltransferase
IUBMB Comments
Requires Mg2+. This membrane-bound protein is located in the plastids . In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.14.142 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.71 (leachianone-G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
The expected taxonomic range for this enzyme is: Sophora flavescens
- 2.5.1.70
-
prenylated
-
sophora
- flavescens
- flavanones
- flavonoids
-
isoprenoid
-
leachianone
-
2'-hydroxy
-
lavandulyl
-
sophoraflavanone
showSynonyms
naringenin 8-dimethylallyltransferase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prenyl diphosphate + (-)-(2S)-naringenin = diphosphate + sophoraflavanone B
reaction mechanism
-
prenyl diphosphate + (-)-(2S)-naringenin = diphosphate + sophoraflavanone B
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase
Requires Mg2+. This membrane-bound protein is located in the plastids [2]. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.14.142 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.71 (leachianone-G 2''-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
158130-09-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,3-dimethylallyl diphosphate + 2'-hydroxynaringenin
diphosphate + leachianone G
-
Substrates: with 2'-hydroxynaringenin, i.e. (S)-2',4',5,7-tetrahydroxy-flavanone, the enzyme shows 3% of the activity with naringenin
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + apigenin
diphosphate + ?
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + hesperetin
diphosphate + (2S)-5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
-
Substrates: i.e. 5,7,3'-trihydroxy-4'-methoxyflavanone
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + hesperetin
diphosphate + ?
Substrates: 52% of the activity with naringenin
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + kaempferol
diphosphate + ?
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + liquiritigenin
diphosphate + ?
Substrates: 102% of the activity with naringenin
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + quercetin
diphosphate + ?
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + taxifolin
diphosphate + (2R,3R)-2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
-
Substrates: i.e. 3,5,7,3',4'-pentahydroxyflavanone
Products: -
Products: -
?
dimethylallyl diphosphate + (-)-(2S)-naringenin
diphosphate + sophoraflavanone B
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-liquiritigenin
diphosphate + isobavachin
-
Substrates: i.e. 4',7-dihydroxyflavanone
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-liquiritigenin
diphosphate + isobavachin
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
8-dimethylallylnaringenin + diphosphate
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
8-dimethylallylnaringenin + diphosphate
-
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
-
Substrates: two possible pathways leading to sophoraflavanone G, overview
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
-
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
-
Substrates: best substrate, the enzyme is enantiospecific for (2S)-naringenin, i.e. (S)-4',5,7-trihydroxy-flavanone, and utilizes 3,3-dimethylallyl diphosphate as sole prenyl donor
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
-
Substrates: i.e. (S)-4',5,7-trihydroxy-flavanone
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, formation of 8-dimethylallyl-, 8-lavandulyl- and 6-dimethylallylflavanones, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: geranyl diphosphate, farnesyl diphosphate, geranylgeranyl diphosphate, and phytyl diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: geranyl diphosphate, farnesyl diphosphate, geranylgeranyl diphosphate, and phytyl diphosphate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + (-)-(2S)-naringenin
diphosphate + sophoraflavanone B
Substrates: -
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
-
Substrates: two possible pathways leading to sophoraflavanone G, overview
Products: -
Products: -
?
3,3-dimethylallyl diphosphate + (2S)-naringenin
diphosphate + sophoraflavanone B
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
no detectable expression in aerial tissues
brenda
additional information
-
no detectable expression in aerial tissues
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular localization of the enzymes involved in the biosynthetic route from naringenin to sophoraflavanone G, overview
-
brenda
the membrane-intrinsic enzyme protein contains a transit peptide sequence at the N-terminus that localizes it to the plastid even when expressed ectopically in heterologous host plants
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
metabolism
the enzyme is involved in the biosynthetic pathway of prenylflavonoid and rutin
additional information
additional information
Tomato fruits overexpressing both N8DT and CHI genes accumulate high levels of rutin compared with wild-type tomato
additional information
Tomato fruits overexpressing both N8DT and CHI genes accumulate high levels of rutin compared with wild-type tomato
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). N8DT1_SOPFL
410
9
46159
Swiss-Prot
other Location (Reliability: 2)
F8WPJ0_SOPFL
410
0
46053
TrEMBL
Mitochondrion (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of chimeric enzymes between narigenin 8-dimethylallyltransferase and isoflavone-specific prenyltransferase G6DT responsible for the prenylation of the genistein at the 6-position, by recombination of amino acid sequences within the loop domains. Chimera SfG2N possesses purely narigenin 8-dimethylallyltransferase activity despite the absence of the N-terminal sequence derived from narigenin 8-dimethylallyltransferase, 243 amino acids. Chimera SfG3N possesses only isoflavone-specific prenyltransferase G6DT activity, although its 33% of the C-terminus is from narigenin 8-dimethylallyltransferase polypeptide. Neither chimeric enzyme can catalyze the prenylation reaction for other types of flavonoid such as kaempferol, apigenin, naringenin chalcone
additional information
-
construction of chimeric enzymes between narigenin 8-dimethylallyltransferase and isoflavone-specific prenyltransferase G6DT responsible for the prenylation of the genistein at the 6-position, by recombination of amino acid sequences within the loop domains. Chimera SfG2N possesses purely narigenin 8-dimethylallyltransferase activity despite the absence of the N-terminal sequence derived from narigenin 8-dimethylallyltransferase, 243 amino acids. Chimera SfG3N possesses only isoflavone-specific prenyltransferase G6DT activity, although its 33% of the C-terminus is from narigenin 8-dimethylallyltransferase polypeptide. Neither chimeric enzyme can catalyze the prenylation reaction for other types of flavonoid such as kaempferol, apigenin, naringenin chalcone
additional information
production of prenylated flavonoids in Solanum lycopersicum as a host plant by means of metabolic engineering through recombinant overexpression of both the naringenin 8-dimethylallyltransferase (N8DT) gene, encoding a prenyltransferase from Sophora flavescens, and the chalcone isomerase (CHI) gene from Nicotiana tabacum cv. Samsun-NN, in transgenic tomato lines. Production of 8-dimethylallyl naringenin in the double transformants, while the production level is lower than N8DT single transformants. Tomato fruits overexpressing both N8DT and CHI genes accumulate high levels of rutin compared with wild-type tomato
additional information
production of prenylated flavonoids in Solanum lycopersicum as a host plant by means of metabolic engineering through recombinant overexpression of both the naringenin 8-dimethylallyltransferase (N8DT) gene, encoding a prenyltransferase from Sophora flavescens, and the chalcone isomerase (CHI) gene from Nicotiana tabacum cv. Samsun-NN, in transgenic tomato lines. Production of 8-dimethylallyl naringenin in the double transformants, while the production level is lower than N8DT single transformants. Tomato fruits overexpressing both N8DT and CHI genes accumulate high levels of rutin compared with wild-type tomato
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene N8DT1, recombinant expression in Solanum lycopersicum transgenic plants contitutively using CaMV 35S promoter
gene N8DT2, recombinant expression in Solanum lycopersicum transgenic plants contitutively using CaMV 35S promoter
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamamoto, H.; Senda, M.; Inoue, K.
Flavanone 8-dimethylallyltransferase in Sophora flavescens cell suspension cultures
Phytochemistry
54
649-655
2000
Sophora flavescens
brenda
Zhao, P.; Inoue, K.; Kouno, I.; Yamamoto, H.
Characterization of leachianone G 2''-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures
Plant Physiol.
133
1306-1313
2003
Sophora flavescens
brenda
Sasaki, K.; Mito, K.; Ohara, K.; Yamamoto, H.; Yazaki, K.
Cloning and characterization of naringenin 8-prenyltransferase, a flavonoid-specific prenyltransferase of Sophora flavescens
Plant Physiol.
146
1075-1084
2008
Sophora flavescens (B1B3P3), Sophora flavescens
brenda
Sasaki, K.; Tsurumaru, Y.; Yazaki, K.
Prenylation of flavonoids by biotransformation of yeast expressing plant membrane-bound prenyltransferase SfN8DT-1
Biosci. Biotechnol. Biochem.
73
759-761
2009
Sophora flavescens
brenda
Sasaki, K.; Tsurumaru, Y.; Yamamoto, H.; Yazaki, K.
Molecular characterization of a membrane-bound prenyltransferase specific for isoflavone from Sophora flavescens
J. Biol. Chem.
286
24125-24134
2011
Sophora flavescens (F8WPJ0), Sophora flavescens
brenda
Kawasaki, T.; Koeduka, T.; Sugiyama, A.; Sasaki, K.; Linley, P.; Shitan, N.; Kumano, T.; Yamamoto, H.; Ezura, H.; Kuzuyama, T.; Yazaki, K.
Metabolic engineering of flavonoids with prenyltransferase and chalcone isomerase genes in tomato fruits
Plant Biotechnol.
31
567-571
2014
Sophora flavescens (B1B3P3), Sophora flavescens (B1B5P4)
-
brenda
EXTERNAL LINKS (specific for EC-Number 2.5.1.70)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
