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(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
+ (+)-4-amino-cyclopent-2-enecarboxylic acid
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
(3S,4R)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone + H2O
?
1,3-benzoxazol-2(3H)-one + H2O
2-aminophenol + CO2
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + (-)-4-amino-cyclopent-2-enecarboxylic acid
low activity with (-)-2-azabicyclo[2.2.1]hept-5-en-3-one, high activity with (+)-2-azabicyclo[2.2.1]hept-5-en-3-one
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carboxylic acid + (1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one
49.8% conversion, 99.7% enantiomeric excess, stereochemical preference to the (1R,4S)-enantiomer
-
-
ir
2-azabicyclo[2.2.1]heptan-3-one + H2O
(1S,3R)-3-aminocyclopentane-1-carboxylic acid + (1S,4R)-2-azabicyclo[2.2.1]heptan-3-one
100% conversion
-
-
ir
2-methyl-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-(methylamino)cyclopent-2-ene-1-carboxylic acid + (1R,4S)-2-methyl-2-azabicyclo[2.2.1]hept-5-en-3-one
49.8% conversion, 99.8% enantiomeric excess
-
-
ir
6-methoxy-1,3-benzoxazol-2(3H)-one + H2O
2-amino-5-methoxyphenol + CO2
racemic 2-azabicyclo [2.2.1] hept-5-en-3-one + H2O
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
additional information
?
-
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
+ (+)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
?
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
+ (+)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
-
enzyme specifically hydrolyzes the (+)-lactam, (1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one, without any actin against the (-)-isomer. Yield is 48%, 97% enantiomeric excess
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
enantiospecific cleavage of (1S,4R)-isomer
99.8% enantiomeric excess
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
enantiospecific cleavage of (1S,4R)-isomer
99.8% enantiomeric excess
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
-
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
-
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
-
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
-
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
50% yield. When racemic 2-azabicyclo[2.2.1]hept-5-en-3-one is used, (1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one is produced with 99% enantiomeric excess
-
?
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
-
50% yield. When racemic 2-azabicyclo[2.2.1]hept-5-en-3-one is used, (1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one is produced with 99% enantiomeric excess
-
?
(3S,4R)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone + H2O
?
-
5.4% yield, 25.4% enantiomeric excess of (3R,4S)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone when racemic substrate is used
-
?
(3S,4R)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone + H2O
?
-
5.4% yield, 25.4% enantiomeric excess of (3R,4S)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone when racemic substrate is used
-
?
1,3-benzoxazol-2(3H)-one + H2O
2-aminophenol + CO2
complete conversion
-
-
?
1,3-benzoxazol-2(3H)-one + H2O
2-aminophenol + CO2
complete conversion
-
-
?
1,3-benzoxazol-2(3H)-one + H2O
2-aminophenol + CO2
complete conversion
-
-
?
1,3-benzoxazol-2(3H)-one + H2O
2-aminophenol + CO2
complete conversion
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
the recombinant enzyme can enantioselectively catalyze the bioresolution of racemic gamma-lactam with a high enantiomeric excess (ee) of 99.8% and enantiomeric ratio (E) above 200
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
i.e. Vince lactam. Wild-type enzyme shows activity on (+)-Vince lactam and (-)-Vince lactam. The mutant enzymes V54S, V54L, V112A, H51A, F110A/V112G and V54T show no activity with (-)-Vince lactam
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
low activity with (-)-2-azabicyclo[2.2.1]hept-5-en-3-one, high activity with (+)-2-azabicyclo[2.2.1]hept-5-en-3-one
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
i.e. Vince lactam. Promiscuous (+)-gamma-lactamase activity of a versatile amidase involved in the nitrile degradation pathway. The kcat for Vince lactam is higher than that of acetamide and acrylamide and lower than that of propionamide and benzamide, indicating that Vince lactam is a moderate preferable substrate
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
i.e. Vince lactam. Promiscuous (+)-gamma-lactamase activity of a versatile amidase involved in the nitrile degradation pathway. The kcat for Vince lactam is higher than that of acetamide and acrylamide and lower than that of propionamide and benzamide, indicating that Vince lactam is a moderate preferable substrate
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
the enzyme forms a single enantiomer of the gamma-bicyclic lactam product which is an important building block for the anti-HIV compound, Abacavir
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
the enzyme forms a single enantiomer of the gamma-bicyclic lactam product which is an important building block for the anti-HIV compound, Abacavir
-
-
?
6-methoxy-1,3-benzoxazol-2(3H)-one + H2O
2-amino-5-methoxyphenol + CO2
complete conversion
-
-
?
6-methoxy-1,3-benzoxazol-2(3H)-one + H2O
2-amino-5-methoxyphenol + CO2
complete conversion
-
-
?
6-methoxy-1,3-benzoxazol-2(3H)-one + H2O
2-amino-5-methoxyphenol + CO2
complete conversion
-
-
?
6-methoxy-1,3-benzoxazol-2(3H)-one + H2O
2-amino-5-methoxyphenol + CO2
complete conversion
-
-
?
racemic 2-azabicyclo [2.2.1] hept-5-en-3-one + H2O
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
A0A5E8GM52
-
-
-
?
racemic 2-azabicyclo [2.2.1] hept-5-en-3-one + H2O
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
A0A5E8GM52
-
-
-
?
additional information
?
-
the enzyme hydrolyzes both (+)- and (-)-gamma-lactam, but with apparently different specificities. Enantioselectivity of the reaction, overview. Enzyme MhIHL preferentially hydrolyzes (+)-gamma-lactam versus (-)-gamma-lactam. The active site of MhIHL is located at the C-termini of the six-stranded beta-sheet, similar to other known structures with substrates. A clear electron density for one ligand is observed in the active site of each protomer in both (+)- and (-)-gamma-lactam-bound MhIHL structures. (+)-gamma-Lactam and (-)-gamma-lactam bind to nearly the same position in MhIHL
-
-
?
additional information
?
-
the enzyme hydrolyzes both (+)- and (-)-gamma-lactam, but with apparently different specificities. Enantioselectivity of the reaction, overview. Enzyme MhIHL preferentially hydrolyzes (+)-gamma-lactam versus (-)-gamma-lactam. The active site of MhIHL is located at the C-termini of the six-stranded beta-sheet, similar to other known structures with substrates. A clear electron density for one ligand is observed in the active site of each protomer in both (+)- and (-)-gamma-lactam-bound MhIHL structures. (+)-gamma-Lactam and (-)-gamma-lactam bind to nearly the same position in MhIHL
-
-
?
additional information
?
-
-
the enzyme hydrolyzes both (+)- and (-)-gamma-lactam, but with apparently different specificities. Enantioselectivity of the reaction, overview. Enzyme MhIHL preferentially hydrolyzes (+)-gamma-lactam versus (-)-gamma-lactam. The active site of MhIHL is located at the C-termini of the six-stranded beta-sheet, similar to other known structures with substrates. A clear electron density for one ligand is observed in the active site of each protomer in both (+)- and (-)-gamma-lactam-bound MhIHL structures. (+)-gamma-Lactam and (-)-gamma-lactam bind to nearly the same position in MhIHL
-
-
?
additional information
?
-
enzyme shows hydrolytic activity on (R)-methyl-3-amino-3 phenylpropanoate
-
-
?
additional information
?
-
the wild-type enzyme cannot hydrolyze classical esterase p-nitrophenyl substrates such as p-nitrophenylbutyrate. It shows weak hydrolysis activizy of (+)-trans-enantiomer of ethyl chrysanthemate. It shows very low activity with ethyl 2-phenylcyclopropanecarboxylate. The wild-type enzyme can hydrolyze ethyl 3-phenylglycidate with high enantioselectivity (hydrolysis of (2S,3R)-ethyl-3-phenylglycidate, enantiomeric excess: 99.5%) but low activity
-
-
?
additional information
?
-
the wild-type enzyme cannot hydrolyze classical esterase p-nitrophenyl substrates such as p-nitrophenylbutyrate. It shows weak hydrolysis activizy of (+)-trans-enantiomer of ethyl chrysanthemate. It shows very low activity with ethyl 2-phenylcyclopropanecarboxylate. The wild-type enzyme can hydrolyze ethyl 3-phenylglycidate with high enantioselectivity (hydrolysis of (2S,3R)-ethyl-3-phenylglycidate, enantiomeric excess: 99.5%) but low activity
-
-
?
additional information
?
-
enzyme shows hydrolytic activity on (R)-methyl-3-amino-3 phenylpropanoate
-
-
?
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12.9 - 61.3
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
34.2
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 25°C
0.378
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 9.0, 30°C
0.19
1,3-benzoxazol-2(3H)-one
pH 7.0, temperature not specified in the publication
12 - 363
2-azabicyclo[2.2.1]hept-5-en-3-one
12.9
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 25°C
17.5
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/Y388H/I336R
22
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/Y388H
26.5
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/I336R
55.9
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme I336R
60.8
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme Y388H/I336R
61.3
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, wild-type enzyme
12
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, wild-type enzyme
18
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95V/V54S
18
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme R162T/V54S
18
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54S
20
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95K/V54S
20.2
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95K/V54L
20.2
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme R162T/V54L
24
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95Q/V54S
26.3
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95V/V54L
28.1
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95Q/V54L
29
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54L
29
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54T
38
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V112A
39
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme F110A/V112G
40
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme H51A
53.9
2-azabicyclo[2.2.1]hept-5-en-3-one
pH and temperature not specified in the publication
363
2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.0
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1.41 - 203.4
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
19.8
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 25°C
4.2
1,3-benzoxazol-2(3H)-one
pH 7.0, temperature not specified in the publication
7.8 - 3145.9
2-azabicyclo[2.2.1]hept-5-en-3-one
1.41
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, wild-type enzyme
1.54
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/Y388H
4.76
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme I336R
7.69
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme Y388H/I336R
8.06
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/I336R
9.04
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/Y388H/I336R
203.4
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 25°C
7.8
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme F110A/V112G
11
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V112A
49
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54T
72
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme H51A
78
2-azabicyclo[2.2.1]hept-5-en-3-one
pH and temperature not specified in the publication
101
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95Q/V54L
120
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95V/V54S
123
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95K/V54L
130
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme R162T/V54S
140
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54S
143
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95Q/V54S
159
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme R162T/V54L
164
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95K/V54S
168
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95V/V54L
190
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54L
200
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, wild-type enzyme
3145.9
2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.023 - 15.77
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
0.58
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 25°C
22
1,3-benzoxazol-2(3H)-one
pH 7.0, temperature not specified in the publication
0.2 - 15.77
2-azabicyclo[2.2.1]hept-5-en-3-one
0.023
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, wild-type enzyme
0.07
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/Y388H
0.085
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme I336R
0.126
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme Y388H/I336R
0.304
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/I336R
0.517
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
37°C, pH 7.8, mutant enzyme V203N/Y388H/I336R
15.77
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 25°C
0.2
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme F110A/V112G
0.3
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V112A
1.45
2-azabicyclo[2.2.1]hept-5-en-3-one
pH and temperature not specified in the publication
1.7
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54T
1.8
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme H51A
3.6
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95Q/V54L
5.9
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95Q/V54S
6.1
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95K/V54L
6.4
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95V/V54L
6.5
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95V/V54S
6.7
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54L
7.2
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme R162T/V54S
7.9
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme R162T/V54L
8.2
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme E95K/V54S
8.2
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, mutant enzyme V54S
15.77
2-azabicyclo[2.2.1]hept-5-en-3-one
pH 7.5, 30°C, wild-type enzyme
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evolution
the isochorismatase-like hydrolase (IHL, Mh33H4-5540, EC 3.3.2.1) with (+)-gamma-lactamase activity constitutes a distinct family of gamma-lactamase
physiological function
gene deletion mutant shows hyphal growth on solid media comparable to the wild-type and significantly reduced growth on media supplied with 1,3-benzoxazol-2(3H)-one and 6-methoxy-1,3-benzoxazol-2(3H)-one
physiological function
gene deletion mutant shows hyphal growth on solid media comparable to the wild-type and significantly reduced growth on media supplied with 1,3-benzoxazol-2(3H)-one and 6-methoxy-1,3-benzoxazol-2(3H)-one
physiological function
(+)-gamma-lactamase catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir
physiological function
-
gene deletion mutant shows hyphal growth on solid media comparable to the wild-type and significantly reduced growth on media supplied with 1,3-benzoxazol-2(3H)-one and 6-methoxy-1,3-benzoxazol-2(3H)-one
-
physiological function
-
gene deletion mutant shows hyphal growth on solid media comparable to the wild-type and significantly reduced growth on media supplied with 1,3-benzoxazol-2(3H)-one and 6-methoxy-1,3-benzoxazol-2(3H)-one
-
additional information
the enzyme crystal structures show that the binding sites of both (+) and (-)-gamma-lactam resemble those of isochorismatase-like hydrolases, but the cover loop conserved in isochorismatase-like hydrolases is lacking in the enzyme, probably resulting in its incomplete enantioselectivity. Structural, biochemical, and molecular dynamics simulation studies demonstrate that the steric clash caused by the binding-site residues, especially the side-chain of Cys111 reduces the binding affinity of (-)-gamma-lactam and possibly the catalytic efficiency, which might explain the different catalytic specificities of the enantiomers of gamma-lactam
additional information
the enzyme crystal structures show that the binding sites of both (+) and (-)-gamma-lactam resemble those of isochorismatase-like hydrolases, but the cover loop conserved in isochorismatase-like hydrolases is lacking in the enzyme, probably resulting in its incomplete enantioselectivity. Structural, biochemical, and molecular dynamics simulation studies demonstrate that the steric clash caused by the binding-site residues, especially the side-chain of Cys111 reduces the binding affinity of (-)-gamma-lactam and possibly the catalytic efficiency, which might explain the different catalytic specificities of the enantiomers of gamma-lactam
additional information
-
the enzyme crystal structures show that the binding sites of both (+) and (-)-gamma-lactam resemble those of isochorismatase-like hydrolases, but the cover loop conserved in isochorismatase-like hydrolases is lacking in the enzyme, probably resulting in its incomplete enantioselectivity. Structural, biochemical, and molecular dynamics simulation studies demonstrate that the steric clash caused by the binding-site residues, especially the side-chain of Cys111 reduces the binding affinity of (-)-gamma-lactam and possibly the catalytic efficiency, which might explain the different catalytic specificities of the enantiomers of gamma-lactam
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C145A
-
mutation in catalytic triad, complete loss of activity
S171A
-
mutation in catalytic triad, complete loss of activity
S195A
-
mutation in catalytic triad, complete loss of activity
C145A
-
mutation in catalytic triad, complete loss of activity
-
S171A
-
mutation in catalytic triad, complete loss of activity
-
S195A
-
mutation in catalytic triad, complete loss of activity
-
C167A
A0A5E8GM52
complete loss of gamma-lactamase activity
D25A
A0A5E8GM52
85% loss of gamma-lactamase activity
K134A
A0A5E8GM52
complete loss of gamma-lactamase activity
N73A
A0A5E8GM52
40% loss of gamma-lactamase activity
Q27A
A0A5E8GM52
complete loss of gamma-lactamase activity
C167A
-
complete loss of gamma-lactamase activity
-
D25A
-
85% loss of gamma-lactamase activity
-
K134A
-
complete loss of gamma-lactamase activity
-
N73A
-
40% loss of gamma-lactamase activity
-
Q27A
-
complete loss of gamma-lactamase activity
-
C111A
(+)-gamma-lactamase activities is totally lost
C118A
complete loss of activity
D13A
mutant enzyme retains 10% (+)-gamma-lactamase activity
D9A
complete loss of activity
E95K/V54S
optimal temperature is 10°C higher compared to wild-type enzyme. Mutant enzyme may be suitable for preparation of the optically pure intermediate (-)-Vince lactam.
F110A/V112G
mutant enzyme shows no activity with (-)-Vince lactam
K78A
(+)-gamma-lactamase activities is totally lost
K84A
9% decrease in activity compared to wild-type
Q11A
20% decrease in activity compared to wild-type
R162T/V54L
optimal temperature is 15°C higher compared to wild-type enzyme
V112A
mutant enzyme shows no activity with (-)-Vince lactam
V54L
mutant enzyme shows no activity with (-)-Vince lactam
V54S
mutant enzyme shows no activity with (-)-Vince lactam
V54T
mutant enzyme shows no activity with (-)-Vince lactam
C145A
mutant enzyme retains 51% of activities relative to the wild-type enzyme
I336R/Y388H
enhanced enzyme activity
K96A
mutant enzyme loses entire hydrolysis activities
Q192N
no improvement of activity as compared to wild-type enzyme
Q192R
no improvement of activity as compared to wild-type enzyme
Q192S/L223Y
high activity and enantioselectivity to phenylglycidate analogs such as methyl 3-methoxyphenylglycidate and methyl 3-phenylglycidate. It shows moderate enantioselectivity to several other chiral compounds. The mutant shows the highest activity towards methyl 2-methylbutyrate but poor enantioselectivity. Catalytic efficiency for gamma-lactamase activity (kcat/Km) of the mutant enzyme shows a slight decrease (about 15%) when compared to that of the wild-type enzyme. When compared to wild-type enzyme, the stability of the mutant enzyme does not change considerably at 50°C. The study employs a three-step method to successfully convert a (+)-gamma-lactamase into an esterase. This three-step method includes the combination of the sequence alignment to recommend the possible substrate, substrate screening to expand the substrate scope, and substrate-enzyme docking to enhance esterase activity
S171A
mutant enzyme loses entire hydrolysis activities
S195A
mutant enzyme loses entire hydrolysis activities
V203N/I336R
enhanced enzyme activity
V203N/I336R/Y388H
enhanced enzyme activity, 21fold higher enzyme efficiency (kcat/KM) compared to the wildtype enzyme. Biotransformation reaches more than 49% conversion and more than 99% enantiomeric excess at 80 °C after 2 h (with the same condition, the wild-type enzyme reached 12.3% conversion). Optimal temperature is 10°C lower than the optimum of the wild-type enzyme
V203N/Y388H
enhanced enzyme activity
C145A
-
mutant enzyme retains 51% of activities relative to the wild-type enzyme
-
I336R/Y388H
-
enhanced enzyme activity
-
K96A
-
mutant enzyme loses entire hydrolysis activities
-
Q192R
-
no improvement of activity as compared to wild-type enzyme
-
S171A
-
mutant enzyme loses entire hydrolysis activities
-
S195A
-
mutant enzyme loses entire hydrolysis activities
-
V203N/I336R
-
enhanced enzyme activity
-
V203N/I336R/Y388H
-
enhanced enzyme activity, 21fold higher enzyme efficiency (kcat/KM) compared to the wildtype enzyme. Biotransformation reaches more than 49% conversion and more than 99% enantiomeric excess at 80 °C after 2 h (with the same condition, the wild-type enzyme reached 12.3% conversion). Optimal temperature is 10°C lower than the optimum of the wild-type enzyme
-
V203N/Y388H
-
enhanced enzyme activity
-
H51A
complete loss of activity
H51A
mutant enzyme shows no activity with (-)-Vince lactam
additional information
compared with expression in Escherichia coli, recombinant lactamase shows improved protein solubility and catalytic activity when expressed in Bacillus subtilis 168
additional information
-
compared with expression in Escherichia coli, recombinant lactamase shows improved protein solubility and catalytic activity when expressed in Bacillus subtilis 168
-
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100
-
12 h, no loss of activity
20
pH 7.0, 1 h, no loss of activity
35
5 h, about 85% loss of activity
40
pH 7.0, 1 h, about 10% loss of activity
41
15 min, 50% loss of activity, wild-type enzyme
48
15 min, 50% loss of activity, mutant enzyme G42T/V56M/G57V
57
15 min, 50% loss of activity, mutant enzyme R162T
58
15 min, 50% loss of activity, mutant enzyme E95V
61
15 min, 50% loss of activity, mutant enzyme E95V/V54L
62
15 min, 50% loss of activity, mutant enzyme E95V/V54S
65
15 min, 50% loss of activity, mutant enzyme E95Q/V54L
66
15 min, 50% loss of activity, mutant enzyme R162T/V54S
67
15 min, 50% loss of activity, mutant enzyme E95Q/V54S
68
15 min, 50% loss of activity, mutant enzyme E95K/V54L
69
15 min, 50% loss of activity, mutant enzyme R162T/V54L
72
15 min, 50% loss of activity, mutant enzyme E95K
80
-
retains 100% of its initial activity for 6 h and retained 52% activity after 10 h
30
pH 7.0, 1 h, about 10% loss of activity
30
5 h, about 55% loss of activity
50
pH 7.0, 1 h, about 65% loss of activity
50
A0A5E8GM52
30 min, soluble enzyme completly loses its activity, enzyme immobilized on macroporous resin using glutaraldehyde cross-linkage loses 10% of its activity
50
1 h, the enzyme can maintain 100% of its original activity when incubated for 1 h
60
pH 7.0, 1 h, about 80% loss of activity
60
A0A5E8GM52
30 min, enzyme immobilized on macroporous resin using glutaraldehyde cross-linkage loses 30% of its activity
60
30 min, 38% residual activity
60
15 min, 50% loss of activity, mutant enzyme E95F
70
15 min, 50% loss of activity, mutant enzyme E95K/V54S
70
15 min, 50% loss of activity, mutant enzyme E95Q
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industry
the enzyme can be a promising candidate of biocatalyst for industrial applications of highly valuable chiral pharmaceutical chemicals
drug development
application of the enzyme in antiviral drug synthesis. The enzyme catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir
drug development
the enzyme can be a promising candidate of biocatalyst for industrial applications of highly valuable chiral pharmaceutical chemicals
drug development
the enzyme is an ideal catalyst for the preparation of carbocyclic nucleosides of pharmaceutical interest. IT can be used in a scalable bioprocess and is an efficient, economical, and environmentally route for producing optically pure (-)-gamma-lactam
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
-
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
-
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
-
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
-
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
-
drug development
-
the enzyme is an ideal catalyst for the preparation of carbocyclic nucleosides of pharmaceutical interest. IT can be used in a scalable bioprocess and is an efficient, economical, and environmentally route for producing optically pure (-)-gamma-lactam
-
drug development
-
the use of gamma-lactamase as a biocatalyst offers an attractive and environmentally friendly approach for the synthesis of a broad range of carbocyclic nucleoside drugs. The enzyme can be used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir
-
synthesis
enantioselective resolution of 100 g/l 2-azabicyclo[2.2.1]hept-5-en-3-one, is achieved with 10 g/l dry cells, resulting in 55.2% conversion and 99% enantiomeric excess of the (-)-gamma-lactam, i.e. (1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one
synthesis
-
the enantiomers of substrate 2-azabicyclo[2.2.1]hept-5-en-3-one (gamma-lactam) are key chiral synthons in the synthesis of antiviral drugs such as carbovir and abacavir
synthesis
(+)-gamma-lactamase catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir
synthesis
mutant enzyme Q192S/L223Y can be employed for the preparation of (-)-gamma-lactam and also for that of (2S,3R)-ethyl 3-phenylglycidate
synthesis
the enzyme may become a potential tool for the production of (-)-gamma-lactam because of its superior physicochemical properties and high enzyme activity
synthesis
A0A5E8GM52
the transformation of an active but unstable mesophilic enzyme into a stable catalyst, achieved by immobilizing the enzyme on macroporous resins, provides a feasible approach for the preparation of optically active (-)-Vince lactam (i.e. 2-azabicyclo [2.2.1] hept-5-en-3-one), which is an important chiral synthon used as an intermediate in organic chemistry
synthesis
-
enantioselective resolution of 100 g/l 2-azabicyclo[2.2.1]hept-5-en-3-one, is achieved with 10 g/l dry cells, resulting in 55.2% conversion and 99% enantiomeric excess of the (-)-gamma-lactam, i.e. (1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one
-
synthesis
-
the enantiomers of substrate 2-azabicyclo[2.2.1]hept-5-en-3-one (gamma-lactam) are key chiral synthons in the synthesis of antiviral drugs such as carbovir and abacavir
-
synthesis
-
the transformation of an active but unstable mesophilic enzyme into a stable catalyst, achieved by immobilizing the enzyme on macroporous resins, provides a feasible approach for the preparation of optically active (-)-Vince lactam (i.e. 2-azabicyclo [2.2.1] hept-5-en-3-one), which is an important chiral synthon used as an intermediate in organic chemistry
-
synthesis
-
mutant enzyme Q192S/L223Y can be employed for the preparation of (-)-gamma-lactam and also for that of (2S,3R)-ethyl 3-phenylglycidate
-
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Xue, T.Y.; Xu, G.C.; Han, R.Z.; Ni, Y.
Soluble expression of (+)-gamma-lactamase in Bacillus subtilis for the enantioselective preparation of abacavir precursor
Appl. Biochem. Biotechnol.
176
1687-1699
2015
Delftia acidovorans (A9BPK4), Delftia acidovorans DSM 14801 (A9BPK4)
brenda
Ren, L.; Zhu, S.; Shi, Y.; Gao, S.; Zheng, G.
Enantioselective resolution of gamma-lactam by a novel thermostable type II (+)-gamma-lactamase from the hyperthermophilic archaeon Aeropyrum pernix
Appl. Biochem. Biotechnol.
176
170-184
2015
Aeropyrum pernix
brenda
Wang, J.; Zhu, Y.; Zhao, G.; Zhu, J.; Wu, S.
Characterization of a recombinant (+)-gamma-lactamase from Microbacterium hydrocarbonoxydans which provides evidence that two enantiocomplementary gamma-lactamases are in the strain
Appl. Microbiol. Biotechnol.
99
3069-3080
2015
Microbacterium hydrocarbonoxydans (A0A077AY47)
brenda
Gao, S.; Zhu, S.; Huang, R.; Lu, Y.; Zheng, G.
Efficient synthesis of the intermediate of abacavir and carbovir using a novel (+)-gamma-lactamase as a catalyst
Bioorg. Med. Chem. Lett.
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2015
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 6
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Kettle, A.J.; Carere, J.; Batley, J.; Benfield, A.H.; Manners, J.M.; Kazan, K.; Gardiner, D.M.
A gamma-lactamase from cereal infecting Fusarium spp. catalyses the first step in the degradation of the benzoxazolinone class of phytoalexins
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Fusarium graminearum (I1R9E4), Fusarium pseudograminearum (K3VFR8), Fusarium pseudograminearum CS3096 (K3VFR8), Fusarium graminearum ATCC MYA-4620 (I1R9E4)
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Zhu, S.; Huang, R.; Gao, S.; Li, X.; Zheng, G.
Discovery and characterization of a second extremely thermostable (+)-gamma-lactamase from Sulfolobus solfataricus P2
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2015
Saccharolobus solfataricus (Q97V26), Saccharolobus solfataricus DSM 1617 (Q97V26)
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Gao, S.; Zhu, S.; Huang, R.; Li, H.; Wang, H.; Zheng, G.
Engineering the enantioselectivity and thermostability of a (+)-?-lactamase from Microbacterium hydrocarbonoxydans for kinetic resolution of Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one)
Appl. Environ. Microbiol.
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Microbacterium hydrocarbonoxydans (A0A0K0XHU0)
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Gao, S.; Huang, R.; Zhu, S.; Li, H.; Zheng, G.
Identification and characterization of a novel (+)-gamma-lactamase from Microbacterium hydrocarbonoxydans
Appl. Microbiol. Biotechnol.
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2016
Microbacterium hydrocarbonoxydans (A0A0K0XHU0), Microbacterium hydrocarbonoxydans
brenda
Gao, S.; Lu, Y.; Li, Y.; Huang, R.; Zheng, G.
Enhancement in the catalytic activity of Sulfolobus solfataricus P2 (+)-?-lactamase by semi-rational design with the aid of a newly established high-throughput screening method
Appl. Microbiol. Biotechnol.
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2019
Saccharolobus solfataricus (P95896), Saccharolobus solfataricus ATCC 35092 (P95896)
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Wang, J.; Zhao, H.; Zhao, G.; Chen, D.; Tao, Y.; Wu, S.
Enhancing the atypical esterase promiscuity of the gamma-lactamase Sspg from Sulfolobus solfataricus by substrate screening
Appl. Microbiol. Biotechnol.
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4077-4087
2019
Saccharolobus solfataricus (P95896), Saccharolobus solfataricus ATCC 35092 (P95896)
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Wang, J.; Zhu, J.; Wu, S.
Immobilization on macroporous resin makes E. coli RutB a robust catalyst for production of (-) Vince lactam
Appl. Microbiol. Biotechnol.
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2015
Escherichia coli (A0A5E8GM52), Escherichia coli JM109 (A0A5E8GM52)
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Li, H.; Zhu, S.; Zheng, G.
Promiscuous (+)-gamma-lactamase activity of an amidase from nitrile hydratase pathway for efficient synthesis of carbocyclic nucleosides intermediate
Bioorg. Med. Chem. Lett.
28
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2018
Rhodococcus erythropolis (Q7DKE4), Rhodococcus erythropolis R4 (Q7DKE4)
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Littlechild, J.A.
Enzymes from Extreme Environments and Their Industrial Applications
Front. Bioeng. Biotechnol.
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Saccharolobus solfataricus, Saccharolobus solfataricus MT4
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Zhu, S.; Zheng, G.
Dynamic kinetic resolution of Vince lactam catalyzed by gamma-lactamases a mini-review
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2018
Aeropyrum pernix, Bradyrhizobium japonicum, Burkholderia cepacia, Delftia acidovorans, Escherichia coli, Pseudomonas fluorescens, Ralstonia solanacearum, Rhodococcus erythropolis, Rhodococcus globerulus, Saccharolobus solfataricus, Nocardia farcinica, Delftia sp., Microbacterium hydrocarbonoxydans, Pseudomonas granadensis, Pseudomonas granadensis B6, Bradyrhizobium japonicum USDA 6, Pseudomonas fluorescens ENZA 22, Ralstonia solanacearum ENZA 20, Rhodococcus erythropolis PR4, Delftia sp. CGMCC 5755
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Su, Y.; Gao, S.; Li, H.; Zheng, G.
Enantioselective resolution of gamma-lactam utilizing a novel (+)-gamma-lactamase from Bacillus thuringiensis
Proc. Biochem.
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2018
Bacillus thuringiensis (Q6HKW3)
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Gao, S.; Zhou, Y.; Zhang, W.; Wang, W.; Yu, Y.; Mu, Y.; Wang, H.; Gong, X.; Zheng, G.; Feng, Y.
Structural insights into the ?-lactamase activity and substrate enantioselectivity of an isochorismatase-like hydrolase from Microbacterium hydrocarbonoxydans
Sci. Rep.
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44542
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Microbacterium hydrocarbonoxydans (A0A0K0XHU0), Microbacterium hydrocarbonoxydans (E3SVR9), Microbacterium hydrocarbonoxydans
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