Any feedback?
Information on EC 2.3.1.93 - 13-hydroxylupanine O-tigloyltransferase and Organism(s) Lupinus albus and UniProt Accession Q5H873
for references in articles please use BRENDA:EC2.3.1.93Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.93 13-hydroxylupanine O-tigloyltransferaseIUBMB Comments
Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA and butanoyl-CoA can act as acyl donors. Involved in the synthesis of lupanine alkaloids.
Specify your search results
The taxonomic range for the selected organisms is: Lupinus albus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
13-hydroxylupanine o-tigloyltransferase, tigloyl-coa:(-)-13alpha-hydroxymultiflorine/(+)-13alpha-hydroxylupanine o-tigloyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
tigloyl-CoA:(-)-13alpha-hydroxymultiflorine/(+)-13alpha-hydroxylupanine O-tigloyltransferase
-
13-hydroxylupanine acyltransferase
-
-
-
-
13-hydroxylupanine O-tigloyltransferase
-
-
-
-
tigloyl-CoA:13-hydroxylupanine O-tigloyltransferase
-
-
-
-
tigloyltransferase, 13-hydroxylupanine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(E)-2-methylcrotonoyl-CoA:13-hydroxylupanine O-2-methylcrotonoyltransferase
Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA and butanoyl-CoA can act as acyl donors. Involved in the synthesis of lupanine alkaloids.
CAS REGISTRY NUMBER
COMMENTARY
85341-00-0
-
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
benzoyl-CoA + 13-alpha-hydroxymultiflorine
CoA + 13-benzoyloxymultiflorine
-
-
-
?
tigloyl-CoA + 13-alpha-hydroxymultiflorine
CoA + 13-tigloyloxymultiflorine
-
-
-
?
3-methylbutyryl-CoA + 13-hydroxylupanine
CoA + 13-(3-methylbutyryl)oxylupanine
-
97% of activity compared to tigloyl-CoA
-
ir
benzoyl-CoA + 13-hydroxylupanine
CoA + 13-benzoyloxylupanine
-
111% of activity compared to tigloyl-CoA
-
ir
butyryl-CoA + 13-hydroxylupanine
CoA + 13-butyryloxylupanine
-
27% of activity compared to tigloyl-CoA
-
ir
propionyl-CoA + 13-hydroxylupanine
CoA + 13-propionyloxylupanine
-
25% of activity compared to tigloyl-CoA
-
ir
valeryl-CoA + 13-hydroxylupanine
CoA + 13-valeryloxylupanine
-
73% of activity compared to tigloyl-CoA
-
ir
tigloyl-CoA + 13-alpha-hydroxymultiflorine
CoA + 13-tigloyloxymultiflorine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
-
?
tigloyl-CoA + 13-alpha-hydroxymultiflorine
CoA + 13-tigloyloxymultiflorine
-
isoform A and B
-
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
ir
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
isoform A and B
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
enzyme is involved in the biosynthesis of quinolizidine alkaloid esters
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
enzyme is involved in the biosynthesis of quinolizidine alkaloid esters
-
?
additional information
?
-
control of quinolizidine alkaloid patterns in a tissue-specific manner
-
-
?
additional information
?
-
-
control of quinolizidine alkaloid patterns in a tissue-specific manner
-
-
?
additional information
?
-
-
lupinine, 4-hydroxylupinine, and cholesterol and acetyl-CoA are no substrates
-
-
?
additional information
?
-
-
baptifoline, epilupinine and lupinine are no substrates
-
-
?
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
tigloyl-CoA + 13-alpha-hydroxymultiflorine
CoA + 13-tigloyloxymultiflorine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
-
?
tigloyl-CoA + 13-alpha-hydroxymultiflorine
CoA + 13-tigloyloxymultiflorine
-
isoform A and B
-
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
tigloyl-CoA is (E)-2-methylcrotonoyl-CoA
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
isoform A and B
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
enzyme is involved in the biosynthesis of quinolizidine alkaloid esters
-
?
tigloyl-CoA + 13-hydroxylupanine
CoA + 13-tigloyloxylupanine
-
enzyme is involved in the biosynthesis of quinolizidine alkaloid esters
-
?
additional information
?
-
control of quinolizidine alkaloid patterns in a tissue-specific manner
-
-
?
additional information
?
-
-
control of quinolizidine alkaloid patterns in a tissue-specific manner
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
cations, e.g. Fe2+, Ca2+, Mg2+, NH4Cl, Fe3+ have no significant influence
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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). HLTT_LUPAL
453
0
51181
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a recombinant protein fused to glutathione S-transferase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wink, M.; Hartmann, T.
Enzymatic synthesis of quinolizidine alkaloid esters: a tigloyl-CoA:13-hydroxylupanine O-tigloyl transferase from Lupinus albus L.
Planta
156
560-565
1982
Lupinus albus, Lupinus polyphyllus, no activity in Conium maculatum, no activity in Cytisus scoparius, no activity in Pisum sativum, no activity in Vicia faba
Suzuki, H.; Murakoshi, I.; Saito, K.
A novel O-tigloyltransferase for alkaloid biosynthesis in plants. Purification, characterization, and distribution in Lupinus plants
J. Biol. Chem.
269
15853-15860
1994
Cytisus scoparius, Lupinus albus, Lupinus hirsutus, Lupinus polyphyllus x Lupinus arboreus, no activity in Lupinus luteus
Okada, T.; Hirai, M.Y.; Suzuki, H.; Yamazaki, M.; Saito, K.
Molecular characterization of a novel quinolizidine alkaloid O-tigloyltransferase: cDNA cloning, catalytic activity of recombinant protein and expression analysis in Lupinus plants
Plant Cell Physiol.
46
233-244
2005
Lupinus albus (Q5H873), Lupinus albus
EXTERNAL LINKS (specific for EC-Number 2.3.1.93)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
