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Information on EC 2.4.1.210 - limonoid glucosyltransferase
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2.4.1.210 limonoid glucosyltransferaseIUBMB Comments
The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin.
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The enzyme appears in viruses and cellular organisms
Synonyms
limonoid udp-glucosyltransferase, limonoid gtase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CitLGT-1
LGTase
limonoid glucosyltransferase
limonoid GTase
-
-
-
-
limonoid UDP-glucosyltransferase
UDP-D-glucose:limonoid glucosyltransferase
-
-
-
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UDP-glucose:limonoid glucosyltransferase
LGTase
-
-
-
-
limonoid glucosyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + limonin = glucosyl-limonin + UDP
the enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin
-
UDP-glucose + limonin = glucosyl-limonin + UDP
catalytic reaction mechanism, overview
-
UDP-glucose + limonin = glucosyl-limonin + UDP
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:limonin glucosyltransferase
The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin.
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CAS REGISTRY NUMBER
COMMENTARY
195836-82-9
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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
UDP-glucose + limonoate A-ring-lactone
UDP + limonin 17-beta-D-glucoside
-
-
-
?
nomilin + UDP-glucose
UDP + nomilin 17-beta-D-glucopyranoside
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-
-
-
?
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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
nomilin + UDP-glucose
UDP + nomilin 17-beta-D-glucopyranoside
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
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modifies tryptophan residues
diethyldicarbonate
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modifies histidine residues and inactivates the enzyme, pseudo first order kinetics. When the histidine modification is reversed by hydroxylamine treatment, 79% of the activity is restored
N-bromosuccinimide
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modifies tryptophan residues and inactivates the enzyme, loss of LGTase activity by NBS treatment is partially protected by pre-incubating the enzyme with excess limonin
additional information
-
inactivation of the enzyme following modification of carboxyl and imidazole moieties is a consequence of a loss in substrate binding and catalysis in the glucosyltransfer reaction. No inhibition by serine modifiying diisopropyl fluorophosphate and cysteine modifying 4-chloromercuribenzoate and iodoacetamide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0813
limonin
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pH 7.8, 37°C, enzyme immobilized covalently on chitosan cross-linked with gluteraldehyde
0.091
limonin
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pH 7.8, 37°C, enzyme immobilized covalently on cellulose carbonate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
enzyme immobilized covalently on chitosan cross-linked with gluteraldehyde (Chito-GA-LGTase)
7.8
7.8
-
soluble enzyme or enzyme immobilized covalently on cellulose carbonate (Ce-Ca-LGTase)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
pH 6.5: about 70% of maximal activity, pH 9.5: about 55% of maximal activity
additional information
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at an acidic pH the D-ring of the substrate that should be in an open form is closed and glycosylation does not occur. The decrease in activity at acidic pH also indicates that an essential residue participates in catalytic functioning while in the unprotonated state
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
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enzyme immobilized covalently on chitosan cross-linked with gluteraldehyde (Chito-GA-LGTase) and enzyme immobilized covalently on cellulose carbonate (Ce-Ca-LGTase)
37
-
soluble enzyme and enzyme immobilized ionically on DEAE-Toyopearl (DE-Tp-LGTase)
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
20°C: about 40% of maximal activity, 60°C: about 40% of maximal activity
20 - 70
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20°C: about 55% of maximal activity, 70°C: about 30% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the genotype of the CitLGT locus in navel orange is homozygous for CitLGT-1 (CitLGT-1/CitLGT-1), whereas. The levels of non-bitter limonoid glucosides in navel orange fruit are quite low at the early-to mid-developmental stage due to a defective CitLGT-2
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-
brenda
the genotype of the CitLGT is heterozygous for CitLGT-1 and CitLGT-2 (CitLGT-1/CitLGT-2)
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of CitLGT-2 is a prerequisite for the accumulation of non-bitter limonoid glucosides at the early- to mid-developmental stage of fruit
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to clade C of flavonoid and limonoid glucosyltransferases
additional information
-
limonoid glucosyltransferase is an enzyme that catalyzes the conversion of bitter limonoid into non-bitter limonoid glucoside while retaining the health benefit of limonoids in the juice
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
pH 7.5, 30 min, free enzyme retains 55% of the activity, enzyme immobilized ionically on DEAE-Toyopearl retains 80% of the activity, enzyme immobilized covalently on cellulose carbonate retains 45% of the activity, enzyme immobilized covalently on chitosan cross-linked with gluteraldehyde retains 40% of the activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized LGTase retains more than 80% activity up to 15 cycles on cellulose carbonate, nine cycles on chitosan and six cycles on DEAE-Toyopearl
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 10 mM Mes-KOH, pH 7 allows frozen storage with full recovery of activity
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4°C, pH 7.5, 10 mM Tris-HCl, enzyme retains 95% of the activity after 3 months, enzyme retains 73% of the activity after 9 months
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cDNA clone encoding limonoid UDP-glucosyltransferase isolated, single copy gene in the citrus genome
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expression in Escherichia coli for sequencing
gene SLLGT, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli and in Pichia pastoris
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
food industry
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Limonoid glucosyltransferase is an enzyme that catalyzes the conversion of bitter limonoid into non-bitter limonoid glucoside while retaining the health benefit of limonoids in the juice. The immobilization of this enzyme in a column can solve the juice bitterness problem
nutrition
agriculture
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whether the CitLGT-2 is present or not, is a useful molecular indicator for predetermining the levels of accumulation of non-bitter limonoid glucosides at the early- to mid-developmental stages of Satsuma mandarin and navel orange fruits. These molecular indicators will make it possible to characterize fruit traits at the seedling stage, resulting in the marker-assisted selection of hybrid progenies to predetermine whether they will accumulate non-bitter limonoid glucosides
agriculture
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whether the CitLGT-2 is present or not, is a useful molecular indicator for predetermining the levels of accumulation of non-bitter limonoid glucosides at the early- to mid-developmental stages of Satsuma mandarin and navel orange fruits. These molecular indicators will make it possible to characterize fruit traits at the seedling stage, resulting in the marker-assisted selection of hybrid progenies to predetermine whether they will accumulate non-bitter limonoid glucosides
agriculture
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gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
agriculture
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gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
agriculture
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gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
agriculture
-
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
agriculture
-
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
nutrition
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limonoid glucosides are important compounds not only for the processing industry but also for the consumer, bitterness due to limonoids is an important economic problem in commercial citrus juice production, limonoid aglycones are converted to nonbitter glucosides by the GTase, enhancement of the limonoid GTase activity through genetic engineering could reduce aglycone concentration, insertion of a gene encoding for GTase into commercial cultivars could create transgenic citrus varieties producing fruits potentially free of limonoid bitterness
nutrition
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exploration of the possibility of using the enzyme in a bioreactor for debittering citrus juice
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sim, M.K.; Lim, B.C.
Purification of limonoid glucosyltransferase from navel orange albedo tissue
Phytochemistry
46
33-37
1997
Citrus aurantium, Citrus limonia, Citrus maxima, Citrus sinensis, Citrus unshiu, Fragaria vesca
-
brenda
Kita, M.; Hirata, Y.; Moriguchi, T.; Endo-Inagaki, T.; Matsumoto, R.; Hasegawa, S.; Suhayda, C.G.; Omura, M.
Molecular cloning and characterization of a novel gene encoding limonoid UDP-glucosyltransferase in Citrus
FEBS Lett.
469
173-178
2000
Citrus sinensis, Citrus unshiu
brenda
Kita, M.; Endo, T.; Shimada, T.; Moriguchi, T.; Hirata, Y.; Hasegawa, S.; Omura, M.
Allelic structures of UDP-glucose:limonoid glucosyltransferase affect limonoid bitterness in Citrus unshiu and C. sinensis
Euphytica
132
87-94
2003
Citrus sinensis, Citrus unshiu
brenda
Karim, M.R.; Hashinaga, F.
Isolation and characterization of limonoid glucosyltransferase from pummelo albedo tissue
Food Chem.
76
431-436
2002
Citrus maxima, Citrus maxima Osbeck
brenda
Endo, T.; Kita, M.; Shimada, T.; Moriguchi, T.; Hidaka, T.; Matsumoto, R.; Hasegawa, S.; Omura, M.
Modification of limonoid metabolism in suspension cell culture of Citrus
Plant Biotechnol.
19
397-403
2002
Citrus sinensis
-
brenda
Karim, M.R.; Hashinaga, F.
Preparation and properties of immobilized pummelo limonoid glucosyltransferase
Proc. Biochem.
38
809-814
2002
Citrus maxima
-
brenda
Zaare-Nahandi, F.; Hosseinkhani, S.; Zamani, Z.; Asadi-Abkenar, A.; Omidbaigi, R.
Delay expression of limonoid UDP-glucosyltransferase makes delayed bitterness in citrus
Biochem. Biophys. Res. Commun.
371
59-62
2008
Citrus aurantium, Citrus limettioides, Citrus sinensis, Citrus unshiu, Citrus x paradisi
brenda
Karim, M.; Hashinaga, F.
Possible role of carboxyl and imidazole groups in the catalysis of pummelo limonoid glucosyltransferase
Chin. J. Catal.
31
1445-1451
2010
Citrus maxima x Citrus paradisi
-
brenda
Devaiah, S.P.; Owens, D.K.; Sibhatu, M.B.; Sarkar, T.R.; Strong, C.L.; Mallampalli, V.K.; Asiago, J.; Cooke, J.; Kiser, S.; Lin, Z.; Wamucho, A.; Hayford, D.; Williams, B.E.; Loftis, P.; Berhow, M.; Pike, L.M.; McIntosh, C.A.
Identification, recombinant expression, and biochemical analysis of putative secondary product glucosyltransferases from Citrus paradisi
J. Agric. Food Chem.
64
1957-1969
2016
Citrus x paradisi (B2YGX8)
brenda
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