3.1.1.43: alpha-amino-acid esterase
This is an abbreviated version!
For detailed information about alpha-amino-acid esterase, go to the full flat file.
Word Map on EC 3.1.1.43
-
3.1.1.43
-
prodrugs
-
synthesis
-
acetobacter
-
turbidans
-
xanthomonas
-
ampicillin
-
valganciclovir
-
cephalexin
-
promoiety
-
beta-lactam
-
carrier-mediated
-
cocaine
-
citri
-
alpha/beta-hydrolase
-
acylases
-
drug development
- 3.1.1.43
-
prodrugs
- synthesis
-
acetobacter
- turbidans
- xanthomonas
- ampicillin
- valganciclovir
- cephalexin
-
promoiety
- beta-lactam
-
carrier-mediated
- cocaine
- citri
-
alpha/beta-hydrolase
- acylases
- drug development
Reaction
Synonyms
AEH, alpha-amino acid ester esterase, alpha-amino acid ester hydrolase, biphenyl hydrolase-like protein, BPH, esterase, alpha-amino acid, VACVase, valacyclovirase
ECTree
Advanced search results
General Information
General Information on EC 3.1.1.43 - alpha-amino-acid esterase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
physiological function
-
hVACVase is a prodrug-activating enzyme for amino acid prodrugs including the antiviral drugs valacyclovir and valganciclovir
additional information
-
the enzyme belongs to the class of hydrolases with alpha/beta-type folding
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Flavobacterium sp. belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Gluconobacter suboxydans belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Mycoplana dimorpha belongs to the first group
evolution
Protaminobacter alboflavus
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Protaminobacter alboflavus belongs to the first group
evolution
Pseudomonas danceae
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas danceae belongs to the first group
evolution
Pseudomonas melanogenum
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas oryzae belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas sp. belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The human enzyme belongs to the second group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The rat enzyme belongs to the second group
evolution
-
the enzyme belongs to the class of hydrolases with alpha/beta-type folding
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
-
evolution
Pseudomonas melanogenum KY3987
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Flavobacterium sp. belongs to the first group
-
evolution
Protaminobacter alboflavus IFO 13221
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Protaminobacter alboflavus belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
-
evolution
Pseudomonas melanogenum IFO 12020
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Gluconobacter suboxydans belongs to the first group
-
evolution
Pseudomonas melanogenum ATCC 17808
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
-
evolution
Pseudomonas melanogenum KY8540
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas oryzae belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Mycoplana dimorpha belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
-
key amino acid residues in the active site are the catalytic triad residues Ser175, His341 and Asp308, residues of the oxyanion hole are Tyr83 and Tyr176, and of the carboxylate cluster are carboxylate groups of Asp209, Glu310 and Asp311. The optimal configuration of residues in the active site occurs with a negative net charge -1 in the carboxylate cluster. Molecular dynamics simulations, docking, and three-dimensional structure homology modeling using the structure of the Xanthomonas campestris enzyme, PDB ID 1MPX, overview
additional information
-
key amino acid residues in the active site are the catalytic triad residues Ser175, His341 and Asp308, residues of the oxyanion hole are Tyr83 and Tyr176, and of the carboxylate cluster are carboxylate groups of Asp209, Glu310 and Asp311. The optimal configuration of residues in the active site occurs with a negative net charge -1 in the carboxylate cluster. Molecular dynamics simulations, docking, and three-dimensional structure homology modeling using the structure of the Xanthomonas campestris enzyme, PDB ID 1MPX, overview
additional information
-
the catalytic triad is formed by residues S174, D307, and H340, and the conserved residue Y82 participates in stabilization of the oxyanion hole
additional information
-
the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341
additional information
-
the catalytic triad is formed by residues Serl22, Asp227, and His255, catalysis involves residues Asp123 and Met52
additional information
-
the catalytic triad is formed by residues Serl22, Asp227, and His255, the acyl pocket by the Asp123 side chain and Tyr175, the oxyanion hole by the Asp123 backbone NH group. The enzyme active center contains a large open groove for the leaving alcohol group of the substrate, the nucleoside-containing group in the hydrolysis of valacyclovir and its analogues
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction, this region affects not only the sub strate specificity of the enzyme but also its activity
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
additional information
-
the enzyme active center contains a large open groove for the leaving alcohol group of the substrate, the nucleoside-containing group in the hydrolysis of valacyclovir and its analogues
additional information
Pseudomonas melanogenum
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction, this region affects not only the sub strate specificity of the enzyme but also its activity
-
additional information
Pseudomonas melanogenum KY3987
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
-
additional information
Pseudomonas melanogenum IFO 12020
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341
-
additional information
Pseudomonas melanogenum ATCC 17808
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
-
additional information
Pseudomonas melanogenum KY8540
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341
-
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction
-
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
-