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Information on EC 2.5.1.122 - 4-O-dimethylallyl-L-tyrosine synthase and Organism(s) Leptosphaeria maculans and UniProt Accession Q6Q874
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2.5.1.122 4-O-dimethylallyl-L-tyrosine synthaseIUBMB Comments
The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.
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Word Map
- 2.5.1.122
- prenyltransferases
- maculans
-
leptosphaeria
-
prenylation
- indole
-
c-prenylations
- dimethylallyltryptophan
-
dmapp
-
thereof
-
regiospecific
- 7-dmats
- l-tryptophan
-
unnatural
-
phytotoxin
- synthesis
- niger
The taxonomic range for the selected organisms is: Leptosphaeria maculans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
tyrpt, tyrosine o-prenyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl diphosphate:L-tyrosine 4-O-dimethylallyltransferase
The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.
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
(2E)-2-methylpenta-2,4-dien-1-yl diphosphate + L-tyrosine
O-[(2E)-2-methylpenta-2,4-dien-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-3-(2-methoxyphenyl)prop-2-en-1-yl trihydrogen diphosphate + L-tyrosine
O-[(2E)-3-(2-methoxyphenyl)prop-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-3-methylpent-2-en-1-yl diphosphate + L-tyrosine
O-[(2E)-3-methylpent-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-3-phenylbut-2-en-1-yl diphosphate + L-tyrosine
O-[(2E)-3-phenylbut-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-3-phenylprop-2-en-1-yl diphosphate + L-tyrosine
O-[(2E)-3-phenylprop-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-5-methylhexa-2,4-dien-1-yl diphosphate + L-tyrosine
O-[(2E)-5-methylhexa-2,4-dien-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-but-2-en-1-yl diphosphate + L-tyrosine
O-[(2E)-but-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E)-penta-2,4-dien-1-yl diphosphate + L-tyrosine
O-[(2E)-penta-2,4-dien-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E,4E)-2-methylhexa-2,4-dien-1-yl diphosphate + L-tyrosine
O-[(2E,4E)-2-methylhexa-2,4-dien-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2E,4E)-5-phenylpenta-2,4-dien-1-yl diphosphate + L-tyrosine
O-[(2E,4E)-5-phenylpenta-2,4-dien-1-yl]-L-tyrosine + diphosphate
-
-
-
?
(2Z)-3-chlorobut-2-en-1-yl diphosphate + L-tyrosine
O-[(2Z)-3-chlorobut-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
2-cyclohexylideneethyl diphosphate + L-tyrosine
O-[2-cyclohexylideneethyl]-L-tyrosine + diphosphate
-
-
-
?
2-methylprop-2-en-1-yl diphosphate + L-tyrosine
O-[2-methylprop-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
2-oxopropyl diphosphate + L-tyrosine
O-[2-oxopropyl]-L-tyrosine + diphosphate
-
-
-
?
2-pentenyl diphosphate + 3-fluoro-DL-tyrosine
diphosphate + 3-fluoro-4-O-(2-pentenyl)-DL-tyrosine
-
20.5% conversion
-
?
2-pentenyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(2-pentenylamino)-L-phenylalanine
-
42.6% conversion
-
?
2-pentenyl diphosphate + alpha-methyl-L-tyrosine
diphosphate + alpha-methyl-4-O-(2-pentenyl)-L-tyrosine
-
33.5% conversion
-
?
2-pentenyl diphosphate + L-tyrosine
diphosphate + 4-O-(2-pentenyl)-L-tyrosine
-
44.3% conversion
-
?
3,3-diphenylprop-2-en-1-yl diphosphate + L-tyrosine
O-[3,3-diphenylprop-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
3-ethylpent-2-en-1-yl diphosphate + L-tyrosine
O-[3-ethylpent-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
benzyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(benzylamino)-L-phenylalanine
-
54.6% conversion
-
?
cyanomethyl diphosphate + L-tyrosine
O-[cyanomethyl]-L-tyrosine + diphosphate
-
-
-
?
cyclohex-1-en-1-ylmethyl diphosphate + L-tyrosine
O-[cyclohex-1-en-1-ylmethyl]-L-tyrosine + diphosphate
-
-
-
?
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
diphosphate + 3-hydroxy-4-dimethylallyloxy-L-phenylalanine
-
88.2% conversion
-
?
dimethylallyl diphosphate + 3,5-dibromo-4-hydroxy-L-phenylalanine
diphosphate + 3,5-dibromo-4-dimethylallyloxy-L-phenylalanine
-
53.3% conversion
-
?
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
diphosphate + 3-fluoro-4-O-dimethylallyl-DL-tyrosine
-
66.5% conversion
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
diphosphate + 3-iodo-4-O-dimethylallyl-L-tyrosine
-
100% conversion
-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(dimethylallylamino)-L-phenylalanine
-
66.1% conversion
-
?
dimethylallyl diphosphate + alpha-methyl-L-tyrosine
diphosphate + alpha-methyl-4-O-dimethylallyl-L-tyrosine
-
89.4% conversion
-
?
dimethylallyl diphosphate + D-tyrosine
diphosphate + 4-O-dimethylallyl-D-tyrosine
-
57.6% conversion
-
?
dimethylallyl diphosphate + L-3,4-dihydroxyphenylalanine
?
16.6% of the activity, compared to L-tyrosine. It is expected that the prenylation takes place at the 4-hydroxyl group. The structure of the product is not determined
-
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 1-(2-methylbut-3-en-2-yl)-L-tryptophan
reverse prenylation
-
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-dimethylallyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-dimethylallyltryptophan
catalytic efficiency for L-tryptophan is 6% compared to catalytic efficiency for L-tyrosine
-
-
?
methylallyl diphosphate + 4-amino-L-phenylalanine
diphosphate + 4-(methylallylamino)-L-phenylalanine
-
34.8% conversion
-
?
methylallyl diphosphate + L-tyrosine
diphosphate + 4-O-methylallyl-L-tyrosine
-
28% conversion
-
?
prop-2-en-1-yl diphosphate + L-tyrosine
O-[prop-2-en-1-yl]-L-tyrosine + diphosphate
-
-
-
?
prop-2-yn-1-yl diphosphate + L-tyrosine
O-[prop-2-yn-1-yl]-L-tyrosine + diphosphate
-
-
-
?
dimethylallyl diphosphate + 3-amino-L-tyrosine
diphosphate + 3-amino-4-O-dimethylallyl-L-tyrosine
-
SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives. 3-Amino-L-tyrosine is prenylated with 108% of the activity compared to L-tyrosine
-
-
?
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
diphosphate + 4-O-dimethylallyl-3-fluoro-DL-tyrosine
-
SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives. 3-Iodo-L-tyrosine is prenylated with 53.6% of the activity compared to L-tyrosine
-
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
diphosphate + 4-O-dimethylallyl-3-iodo-L-tyrosine
-
SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives. 3-Iodo-L-tyrosine is prenylated with 27.3% of the activity compared to L-tyrosine
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
99.3% conversion
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
first committed step in the biosynthesis of the phytotoxin sirodesmin PL
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
the enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
no activity with cyclo-L-Tyr-L-Ser, L-Phe, 4-hydroxybenzoate or 4-coumarate
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
the enzyme is involved in biosynthesis of sirodesmin PL
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
SirD catalyzes the regiospecific O-prenylation at position C4 of tyrosine and derivatives
-
-
?
additional information
?
-
SirD also prenylates L-Trp, resulting in the formation of 7-dimethylallyltryptophan. SirD catalyses the C-prenylation of L-Trp, in addition to the O-prenylation of L-Tyr, cf. EC 2.5.1.34
-
-
?
additional information
?
-
-
SirD also prenylates L-Trp, resulting in the formation of 7-dimethylallyltryptophan. SirD catalyses the C-prenylation of L-Trp, in addition to the O-prenylation of L-Tyr, cf. EC 2.5.1.34
-
-
?
additional information
?
-
the catalytic erfficiency with 4-mercapto-L-phenylalanine, 4-methoxy-L-tryptophan and 7-methyl-L-tryptophan is less than 1% of the reaction with L-tyrosine
-
-
?
additional information
?
-
-
the catalytic erfficiency with 4-mercapto-L-phenylalanine, 4-methoxy-L-tryptophan and 7-methyl-L-tryptophan is less than 1% of the reaction with L-tyrosine
-
-
?
additional information
?
-
in presence of unnatural dimethylallyl diphosphate analogs such as methylallyl, 2-pentenyl and benzyl diphosphate for alkylation, or benzylation of the indole ring enzyme catalyzes the regiospecific O- or N-alkylation or benzylation at position C4 of the aromatic ring
-
-
?
additional information
?
-
-
in presence of unnatural dimethylallyl diphosphate analogs such as methylallyl, 2-pentenyl and benzyl diphosphate for alkylation, or benzylation of the indole ring enzyme catalyzes the regiospecific O- or N-alkylation or benzylation at position C4 of the aromatic ring
-
-
?
additional information
?
-
-
SirD also catalyses the C-prenylation of L-Trp derivatives, in addition to the O-prenylation
-
-
?
additional information
?
-
-
no activity with 1-naphthol, 1,6-dihydroxynaphthalene, 1,7-dihydroxynaphthalene, 2,6-dihydroxynaphthalene, 2,7-dihydroxynaphthalene, 3,5-dihydroxy-2-naphthoic acid, and 3,7-dihydroxy-2-naphthoic acid
-
-
?
NATURAL SUBSTRATE
NATURAL 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
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
first committed step in the biosynthesis of the phytotoxin sirodesmin PL
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
the enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
the enzyme is involved in biosynthesis of sirodesmin PL
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
5 mM, 1.4fold activation compared to activity without additives
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
(2E)-2-methylpenta-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.73
(2E)-5-methylhexa-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.12
(2E,4Z)-2-methylhexa-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.22
2-pentenyl diphosphate
cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C
0.75
benzyl diphosphate
cosubstrate 4-aminophenylalanine, pH 7.5, 37°C
0.13
methylallyl diphosphate
cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C
0.23
dimethylallyl diphosphate
with L-tyrosine as cosubstrate, at pH 7.5 and 35°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00367
(2E)-2-methylpenta-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.00167
(2E)-5-methylhexa-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.00083
(2E)-penta-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.0123
(2E,4Z)-2-methylhexa-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.00067
(2Z)-3-chlorobut-2-en-1-yl diphosphate
at pH 7.5 and 35°C
0.002
2-pentenyl diphosphate
cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C
0.028
benzyl diphosphate
cosubstrate 4-aminophenylalanine, pH 7.5, 37°C
0.003
methylallyl diphosphate
cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C
0.683
dimethylallyl diphosphate
with L-tyrosine as cosubstrate, at pH 7.5 and 35°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0217
(2E)-2-methylpenta-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.0023
(2E)-5-methylhexa-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.1017
(2E,4Z)-2-methylhexa-2,4-dien-1-yl diphosphate
at pH 7.5 and 35°C
0.0167
(2Z)-3-chlorobut-2-en-1-yl diphosphate
at pH 7.5 and 35°C
0.098
2-pentenyl diphosphate
cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C
0.037
benzyl diphosphate
cosubstrate 4-aminophenylalanine, pH 7.5, 37°C
0.021
methylallyl diphosphate
cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C
2.97
dimethylallyl diphosphate
with L-tyrosine as cosubstrate, at pH 7.5 and 35°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involved in biosynthesis of the epidithiopiperazinedione toxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans
physiological function
-
the enzyme is involved in biosynthesis of sirodesmin PL
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). SIRD_LEPMC
448
0
50986
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the broad alkyl donor specificity of SirD opens the door for the interrogation of the alkyl donor specificity of other prenyltransferases for potential utility as biocatalysts for differential alkylation applications
synthesis
-
the specific 4-O-prenylation of tyrosine derivatives by SirD could find usage for production of prenylated tyrosine derivatives by chemoenzymatic synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, X.; Xie, X.; Li, S.M.
Substrate promiscuity of secondary metabolite enzymes: prenylation of hydroxynaphthalenes by fungal indole prenyltransferases
Appl. Microbiol. Biotechnol.
92
737-748
2011
Leptosphaeria maculans
Rudolf, J.D.; Poulter, C.D.
Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives
ACS Chem. Biol.
8
2707-2714
2013
Leptosphaeria maculans (Q6Q874), Leptosphaeria maculans
Zou, H.X.; Xie, X.; Zheng, X.D.; Li, S.M.
The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations
Appl. Microbiol. Biotechnol.
89
1443-1451
2011
Leptosphaeria maculans
Kremer, A.; Li, S.M.
A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL
Microbiology
156
278-286
2010
Leptosphaeria maculans (Q6Q874), Leptosphaeria maculans
Yu, H.; Liebhold, M.; Xie, X.; Li, S.M.
Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate
Appl. Microbiol. Biotechnol.
99
7115-7124
2015
Aspergillus niger, Leptosphaeria maculans (Q6Q874), Leptosphaeria maculans
Bandari, C.; Scull, E.M.; Masterson, J.M.; Tran, R.H.Q.; Foster, S.B.; Nicholas, K.M.; Singh, S.
Determination of alkyl-donor promiscuity of tyrosine-O-prenyltransferase SirD from Leptosphaeria maculans
ChemBioChem
18
2323-2327
2017
Leptosphaeria maculans (Q6Q874), Leptosphaeria maculans
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