3.2.1.40: alpha-L-rhamnosidase
This is an abbreviated version!
For detailed information about alpha-L-rhamnosidase, go to the full flat file.
Word Map on EC 3.2.1.40
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3.2.1.40
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l-rhamnose
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decumbens
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debittering
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hesperidin
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prunin
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grapefruit
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albidus
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food industry
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erubescens
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eupenicillium
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rhamnosylated
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hesperidinase
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beta-d-glucosidase
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nutrition
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alpha-1,2
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gellan
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synthesis
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biotechnology
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industry
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drug development
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degradation
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pharmacology
- 3.2.1.40
- l-rhamnose
- decumbens
-
debittering
- hesperidin
- prunin
- grapefruit
- albidus
- food industry
- erubescens
- eupenicillium
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rhamnosylated
-
hesperidinase
- beta-d-glucosidase
- nutrition
-
alpha-1,2
- gellan
- synthesis
- biotechnology
- industry
- drug development
- degradation
- pharmacology
Reaction
Synonyms
alpha-L-rhamnosidase, alpha-L-rhamnosidase A, alpha-L-rhamnosidase B, alpha-L-rhamnosidase N, alpha-L-rhamnosidase Ram A, alpha-L-rhamnosidase T, alpha-RHA, AoRha, AorhaA, BtRha, BtRha78A, DtRha, EC 3.2.1.66, GH106 alpha-L-rhamnosidase, gypenoside-alpha-L-rhamnosidase, KoRha, L-rhamnosidase, More, naringinase, pnp-rhamnohydrolase, RamA, RHA-P, RhaA, RhaB, RhaB1, RhaB2, RhaL1, Rham, rhamnosidase, alpha -L-, RhmA, saponin-alpha-L-rhamnosidase
ECTree
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Engineering
Engineering on EC 3.2.1.40 - alpha-L-rhamnosidase
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W261Y
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mutant enzyme with improved product yield in synthesis of rhamnose-containing chemicals through reverse hydrolysis reaction with rhamnose as glycosyl donor. Reverse hydrolysis is accelerated with 43.7% in relative yield compared to the wild-type enzyme. Based on 3D structural modeling, it is supposed that the improved yield of mutant W261Y is due to the adjustment of the spatial position of the putative catalytic acid residue Asp257. Mutant W261Y also exhibits a shift in the pH-activity profile in hydrolysis reaction, indicating that introducing of a polar residue in the active site cavity may affect the catalysis behavior of the enzyme
Y302F
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mutant enzyme with improved product yield in synthesis of rhamnose-containing chemicals through reverse hydrolysis reaction with rhamnose as glycosyl donor. Reverse hydrolysis is accelerated with 33.3% in relative yield compared to the wild-type enzyme
Y316F
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mutant enzyme with improved product yield in synthesis of rhamnose-containing chemicals through reverse hydrolysis reaction with rhamnose as glycosyl donor. Reverse hydrolysis is accelerated with 19.8% in relative yield compared to the wild-type enzyme
K406R/K573R
to improve the thermostability of the enzyme multiple arginine residues are introduced into the r-Rha1 sequence to replace several lysine residues that located on the surface of the folded enzyme. Hinted by in silico analysis, five surface Lys residues (K134, K228, K406, K440, K573) are targeted to produce a list of 5 single-residue mutants and 4 multiple-residue mutants using site-directed mutagenesis. Among these mutants, K406R/K573R shows the best thermostability improvement. The half-life of this mutant's enzyme activity increased 3 h at 60°C, 23 min at 65°C, and 3.5 min at 70°C, when compared with the wild type. With the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
V529A
mutant enzyme with improved thermostability, improved substrate affinity and better resistance to the inhibition of glucose
K406R/K573R
Aspergillus niger JMU-TS528
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to improve the thermostability of the enzyme multiple arginine residues are introduced into the r-Rha1 sequence to replace several lysine residues that located on the surface of the folded enzyme. Hinted by in silico analysis, five surface Lys residues (K134, K228, K406, K440, K573) are targeted to produce a list of 5 single-residue mutants and 4 multiple-residue mutants using site-directed mutagenesis. Among these mutants, K406R/K573R shows the best thermostability improvement. The half-life of this mutant's enzyme activity increased 3 h at 60°C, 23 min at 65°C, and 3.5 min at 70°C, when compared with the wild type. With the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
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V529A
Aspergillus niger JMU-TS528
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mutant enzyme with improved thermostability, improved substrate affinity and better resistance to the inhibition of glucose
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D594Q
half-life at 70°C is prolonged by 2.1fold. Analysis of the 3D structure shows that in the thermostable variants the number of hydrogen bonds and salt bridges is increased, explaining the enhanced thermostability. The KM value for 4-nitrophenyl-alpha-L-rhamnopyranoside decreases by 4.0%. The kcat/KM value increases by 15.5%. The mutant enzyme exhibits markedly improved isoquercitrin yield at 70°C that increases by 13.5%
D594Q/G827K
half-life at 70°C is prolonged by 2.3fold. Analysis of the 3D structure shows that in the thermostable variants the number of hydrogen bonds and salt bridges is increased, explaining the enhanced thermostability. The KM value for 4-nitrophenyl-alpha-L-rhamnopyranoside decreases by 3.8%. The kcat/KM value increases by 9.2%. The mutant enzyme exhibits markedly improved isoquercitrin yield at 70°C that increases by 11.0%
D567N
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
D579N
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
E572Q
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
E841Q
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
D567N
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mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
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D579N
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mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
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E572Q
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mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
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E841Q
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mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
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D330A
2350fold reduction in specific activity as compared to the wild-type enzyme
D335A
560fold reduction in specific activity as compared to the wild-type enzyme
D335E
2770fold reduction in specific activity as compared to the wild-type enzyme
D335N
1170fold reduction in specific activity as compared to the wild-type enzyme
D342A
7670fold reduction in specific activity as compared to the wild-type enzyme
E595A
6970fold reduction in specific activity as compared to the wild-type enzyme
E595Q
19170fold reduction in specific activity as compared to the wild-type enzyme
H620A
40fold reduction in specific activity as compared to the wild-type enzyme
R334A
280fold reduction in specific activity as compared to the wild-type enzyme
W339A
1230fold reduction in specific activity as compared to the wild-type enzyme
W440A
530fold reduction in specific activity as compared to the wild-type enzyme
Y383A
740fold reduction in specific activity as compared to the wild-type enzyme
D330A
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2350fold reduction in specific activity as compared to the wild-type enzyme
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D335A
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560fold reduction in specific activity as compared to the wild-type enzyme
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D335N
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1170fold reduction in specific activity as compared to the wild-type enzyme
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D342A
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7670fold reduction in specific activity as compared to the wild-type enzyme
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R334A
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280fold reduction in specific activity as compared to the wild-type enzyme
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D552A
D763A
kcat/KM value is 65% of the wild-type value. This reduced catalytic efficiency is mainly due to a significative variation in the turnover number, defined by the kcat value, for which a 34% decrease is observed
kcat/KM value is 21% of the wild-type value. A 82% decrease in kcat is retrieved for the mutant enzyme, while the KM is similar within the experimental error