3.5.2.B2: (+)-gamma-lactamase
This is an abbreviated version!
For detailed information about (+)-gamma-lactamase, go to the full flat file.
Word Map on EC 3.5.2.B2
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3.5.2.B2
-
drug development
-
synthesis
-
abacavir
-
enantioselective
-
sulfolobus
-
microbacterium
-
carbovir
-
biuret
-
racemic
-
enantiomeric
-
solfataricus
-
carbocyclic
-
nucleoside
-
japonicum
-
bradyrhizobium
-
industry
- 3.5.2.B2
- drug development
- synthesis
- abacavir
-
enantioselective
-
sulfolobus
-
microbacterium
-
carbovir
- biuret
-
racemic
-
enantiomeric
- solfataricus
-
carbocyclic
- nucleoside
- japonicum
-
bradyrhizobium
- industry
Reaction
Synonyms
(+) gamma-lactamase, (+)-gamma-lactamase, BJ6T_02120, Daci_0225, Delm, FDB1, FGSG_00079, FPSE_08124, IHL, isochorismatase-like hydrolase, Mh33H4-5540, MhIHL, Mhpg, RutB, Sslact, SSO2810, Sspg, SYJ322B5
ECTree
3.5.2.B2 (+)-gamma-lactamaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.5.2.B2 - (+)-gamma-lactamase
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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
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
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
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
(+)-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
-
-
?
