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
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drug development
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synthesis
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abacavir
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enantioselective
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sulfolobus
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microbacterium
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carbovir
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biuret
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racemic
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enantiomeric
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solfataricus
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carbocyclic
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nucleoside
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japonicum
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bradyrhizobium
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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
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General Information
General Information on EC 3.5.2.B2 - (+)-gamma-lactamase
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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
additional information
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
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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
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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