3.2.1.149: beta-primeverosidase

This is an abbreviated version!
For detailed information about beta-primeverosidase, go to the full flat file.

Reaction

Synonyms

4-methylumbelliferyl-beta-D-glucopyranoside:beta-glucosidase, arbutinase, ary beta-glucosidase, beta-D-glucosidase, beta-D-glucoside glucohydrolase, beta-glucosidase, beta-glucoside hydrolase, beta-primeverosidase, diglycoside-specific beta-primeverosidase, p-nitrophenyl beta-glucosidase, primeverosidase, vicianase

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.149 beta-primeverosidase

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Results	in table
7	AA Sequence
1	Application
2	CAS Registry Number
8	Cloned(Commentary)
1	Crystallization (Commentary)
7	General Information
5	Inhibitors
3	Ki Value [mM]
13	KM Value [mM]
5	Localization
12	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
23	Organism
1	Pathway
6	PDB ID
8	pH Optimum
2	pH Range
4	pH Stability
3	pI Value
1	Posttranslational Modification
10	Purification (Commentary)
1	Reaction
1	Reaction Type
17	Reference
13	Source Tissue
16	Specific Activity [micromol/min/mg]
81	Substrates and Products (Substrate)
7	Subunits
19	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
3	Temperature Range [°C]
4	Temperature Stability [°C]
6	Turnover Number [1/s]

General Information

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General Information on EC 3.2.1.149 - beta-primeverosidase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

Camellia sinensis

Q7X9A9

phylogenetic analysis and tree, the enzyme belongs to the glycosyl hydrolase family 1, GH1. All GH1 family beta-Glus in Camellia sinensis contain the same PfamB domain (PB027112) in the N-terminus, followed by a PfamA domain (PF00232, glyco_hydro_1)

753640

physiological function

4 entries

additional information

2 entries

physiological function

Camellia sinensis

Q7X9A9

beta-primeverosidase is a disaccharide-specific beta-glycosidase in tea leaves. This enzyme is involved in aroma formation during the manufacturing process of oolong tea and black tea. The enzyme hydrolyzes beta-primeveroside at the beta-glycosidic bond of primeverose to aglycone, and releases aromatic alcoholic volatiles of aglycones

732136

physiological function

Camellia sinensis

Q7X9A9

aroma of oolong tea does not result from hydrolysis of glycosidically bound volatiles (GBVs) by beta-primeverosidase. beta-Primeverosidase is located in the leaf cell wall. The cell wall remains intact during the enzyme-active manufacturing process. After the leaf cell disruption, GBV content is reduced. These findings reveal that, during the enzyme-active process of oolong tea, nondisruption of the leaf cell walls results in impossibility of interaction of GBVs and beta-glycosidases. Indole, jasmine lactone, and trans-nerolidol are characteristic volatiles produced from the manufacturing process. Interestingly, the contents of the three volatiles is reduced after the leaf cell disruption, suggesting that mechanical damage via the cell disruption, which is similar to black tea manufacturing, does not induce accumulation of the three volatiles. In addition, 11 volatiles with flavor dilution factor 4 and above are identified as relatively potent odorants in the oolong tea. These results suggest that enzymatic hydrolysis of GBVs is not involved in the formation of volatiles of oolong tea, and some characteristic volatiles with potent odorants are produced from the manufacturing process

753954

physiological function

Ipomoea batatas

-

effect of diglycoside-specific beta-primeverosidase on aroma formation during sweet potato shochu (hard liquor) manufacturing, overview. Exogenously added beta-glycosidase primarily cleaves between primeveroside (a disaccharide of Xylbeta1-6Glc) and its aromatic aglycon volatiles. beta-Glycosidase (beta-primeverosidase) is involved in monoterpene alcohol (MTA) production in sweet potato shochu. Various aroma compounds in sweet potato shochu released by beta-primeverosidase might be involved in host defences against pathogenic organisms

754216

physiological function

Camellia sinensis

Q7X9A9

many tea aroma compounds are present as glycosidically conjugated forms in tea leaves, and can be hydrolyzed by beta-glucosidase (beta-Glu) and beta-primeverosidase. beta-Primeverosidase hydrolyzes beta-primeverosidically bound volatiles to free volatiles. In tea leaves, beta-primeverosidase and beta-Glus are the main enzymes involved in the transformation of glycosidically bound volatiles (GBVs) into free volatiles. Disruption of the tea leaf cells is essential for the interaction of substrates (GBVs occur in vacuoles) and enzymes (beta-primeverosidase localized in cell walls)

753640

additional information

Camellia sinensis

Q7X9A9

three-dimensional structures of the enzyme in apo and complex forms with N-beta-primeverosylamidines, overview. Three subsites in the active site: subsite -2 specific for 6-O-beta-D-xylopyranosyl, subsite -1 well conserved among beta-glucosidases and specific for beta-D-glucopyranosyl, and wide subsite +1 for hydrophobic aglycone. Glu470, Ser473, and Gln477 act as the specific hydrogen bond donors for 6-O-beta-D-xylopyranosyl in subsite +2. On the other hand, subsite +1 is a large hydrophobic cavity that accommodates various aromatic aglycones. Tight binding of the disaccharide in the deep active site, overview

732136

additional information

Camellia sinensis

Q7X9A9

identification of potent odorants in oolong tea, overview

753954