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Literature summary for 2.4.1.210 extracted from

  • Karim, M.; Hashinaga, F.
    Possible role of carboxyl and imidazole groups in the catalysis of pummelo limonoid glucosyltransferase (2010), Chin. J. Catal., 31, 1445-1451.
No PubMed abstract available
Search for more literature for 2.4.1.210

Application

Application Comment Organism
food industry 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 Citrus maxima x Citrus paradisi

Inhibitors

Inhibitors Comment Organism Structure
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide modifies tryptophan residues Citrus maxima x Citrus paradisi
3-nitro-L-tyrosine ethylester modifies tryptophan residues Citrus maxima x Citrus paradisi
citraconic anhydride modifies lysine residues Citrus maxima x Citrus paradisi
diethyldicarbonate 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 Citrus maxima x Citrus paradisi
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 Citrus maxima x Citrus paradisi
N-bromosuccinimide 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 Citrus maxima x Citrus paradisi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.065
-
 limonin pH 7.0-8.4, 25°C Citrus maxima x Citrus paradisi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucose + limonin Citrus maxima x Citrus paradisi
-
 glucosyl-limonin + UDP
-
 ?

Organism

Organism UniProt Comment Textmining
Citrus maxima x Citrus paradisi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
UDP-glucose + limonin + H2O = glucosyl-limonin + UDP catalytic reaction mechanism, overview Citrus maxima x Citrus paradisi
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + limonin
-
 Citrus maxima x Citrus paradisi glucosyl-limonin + UDP
-
 ?

Synonyms

Synonyms Comment Organism
LGTase
-
 Citrus maxima x Citrus paradisi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Citrus maxima x Citrus paradisi

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
91.7
-
 limonin pH 7.0-8.4, 25°C Citrus maxima x Citrus paradisi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
 Citrus maxima x Citrus paradisi

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 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 Citrus maxima x Citrus paradisi
5.5 9.5 activity range Citrus maxima x Citrus paradisi

General Information

General Information Comment Organism
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 Citrus maxima x Citrus paradisi