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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-2-amino-delta-valerolactam
L-2-amino-delta-valerolactam
-
best substrate
-
-
r
D-2-amino-omega-octalactam
L-2-amino-omega-octalactam
-
1.78% activity compared to D-2-aminohexano-6-lactam
-
-
r
D-2-aminobutyric acid amide
L-2-aminobutyric acid amide
-
0.19% activity compared to D-2-aminohexano-6-lactam
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
D-alanine amide
L-alanine amide
-
2.12% activity compared to D-2-aminohexano-6-lactam
-
-
r
D-alpha-amino-beta-caprolactam
DL-alpha-amino-beta-caprolactam
-
-
-
-
?
L-2-amino-delta-valerolactam
D-2-amino-delta-valerolactam
-
17.2% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-2-amino-omega-octalactam
D-2-amino-omega-octalactam
-
1.41% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-2-aminobutyric acid amide
D-2-aminobutyric acid amide
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
L-alanine amide
D-alanine amide
L-alpha-Amino-beta-thio-epsilon-caprolactam
D-alpha-Amino-beta-thio-epsilon-caprolactam
-
racemized more than 3times faster and binds about 4fold stronger to the enzyme than L-alpha-amino-epsilon-caprolactam
-
-
?
L-alpha-Amino-delta-valerolactam
D-alpha-Amino-delta-valerolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
L-leucine amide
D-leucine amide
L-methionine amide
D-methionine amide
L-phenylalanine amide
D-phenylalanine amide
L-phenylglycine amide
D-phenylglycine amide
L-serine amide
D-serine amide
L-valine amide
D-valine amide
additional information
?
-
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
preferred substrate
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
preferred substrate
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
high activity
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
L-2-aminobutyric acid amide
D-2-aminobutyric acid amide
-
-
-
-
r
L-2-aminobutyric acid amide
D-2-aminobutyric acid amide
-
0.08% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
high activity
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
high activity
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
high activity
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
-
?
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
-
r
L-alanine amide
D-alanine amide
-
0.77% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
r
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
r
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
r
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
r
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
?
L-leucine amide
D-leucine amide
-
-
-
r
L-leucine amide
D-leucine amide
-
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-serine amide
D-serine amide
-
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
-
r
additional information
?
-
-
the enzyme catalyzes alpha-proton exchange of the substrate with deuterium during racemization in deuterium oxide
-
-
?
additional information
?
-
-
no racemization activity is observed with dipeptides or amino acid derivatives, such as L-Ala-D-Ala, D-Ala-L-Ala, L-alanylglycine, L-phenylglycine, or L-alanine methylester
-
-
?
additional information
?
-
The enzyme acts on a broad range of amino acid amides, particularly unbranched amino acid amides including L-alanine amide and L-serine amide. No activity with L-tyrosine amide
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-leucine amide, and L-phenylglycine amide, and not active on L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
-
the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene Oant_4493 is an aminotransferase class-III (UniProt ID A6X7I5), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene Oant_4493 is an aminotransferase class-III (UniProt ID A6X7I5), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-tyrosine amide, and L-phenylglycine amide, and not active on L-leucine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-tyrosine amide, and L-phenylglycine amide, and not active on L-leucine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
-
the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
-
the enzyme encoded by gene CSE45_2055 is a 2,2-dialkylglycine decarboxylase, EC 4.1.1.64 (UniProt ID D0D2T1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene CSE45_2055 is a 2,2-dialkylglycine decarboxylase, EC 4.1.1.64 (UniProt ID D0D2T1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
The enzyme acts on a broad range of amino acid amides, particularly unbranched amino acid amides including L-alanine amide and L-serine amide. No activity with L-tyrosine amide
-
-
?
additional information
?
-
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-leucine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
-
the enzyme acts on 2-aminohexano-6-lactam and 2-amino acid amides, the enzyme prefers the D-enantiomers as substrates
-
-
?
additional information
?
-
-
the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme encoded by gene JNB_04915 is a Putative aminotransferase protein (UniProt ID A3TM80), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme encoded by gene Mesop_2670 is an aminotransferase class-III (UniProt ID F7Y223), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme encoded by gene Mvan_2918 is an aminotransferase (EC 2.6.1, UniProt ID A1T974), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, L-serine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme encoded by gene Smed_5339 is an aminotransferase class-III (UniProt ID A6UKD1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-tyrosine amide, and L-phenylglycine amide, and not active on L-leucine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme encoded by gene SM0020_01805 is an acetylornithine transaminase (UniProt ID H0FT96), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SM0020_01805 is an acetylornithine transaminase (UniProt ID H0FT96), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SMc02413 is a class-III pyridoxal-phosphate-dependent aminotransferase family protein, UniProt ID Q92MM4,that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SMc02413 is a class-III pyridoxal-phosphate-dependent aminotransferase family protein, UniProt ID Q92MM4,that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-leucine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-leucine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
additional information
?
-
the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
r
additional information
?
-
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
-
r
additional information
?
-
-
the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene Oant_4493 is an aminotransferase class-III (UniProt ID A6X7I5), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene Oant_4493 is an aminotransferase class-III (UniProt ID A6X7I5), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene CSE45_2055 is a 2,2-dialkylglycine decarboxylase, EC 4.1.1.64 (UniProt ID D0D2T1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene CSE45_2055 is a 2,2-dialkylglycine decarboxylase, EC 4.1.1.64 (UniProt ID D0D2T1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
-
the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene JNB_04915 is a Putative aminotransferase protein (UniProt ID A3TM80), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene Mesop_2670 is an aminotransferase class-III (UniProt ID F7Y223), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene Mvan_2918 is an aminotransferase (EC 2.6.1, UniProt ID A1T974), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene Smed_5339 is an aminotransferase class-III (UniProt ID A6UKD1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SM0020_01805 is an acetylornithine transaminase (UniProt ID H0FT96), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SM0020_01805 is an acetylornithine transaminase (UniProt ID H0FT96), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SMc02413 is a class-III pyridoxal-phosphate-dependent aminotransferase family protein, UniProt ID Q92MM4,that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
the enzyme encoded by gene SMc02413 is a class-III pyridoxal-phosphate-dependent aminotransferase family protein, UniProt ID Q92MM4,that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.04
-
purified recombinant enzyme, substrate L-valine amide, pH 7.5, 30°C
0.06
purified recombinant enzyme, substrate L-valine amide, pH 7.5, 30°C
0.2
purified recombinant enzyme, substrate L-phenylalanine, pH 7.5, 30°C
0.3
-
purified recombinant enzyme, substrate L-phenylalanine, pH 7.5, 30°C
0.8
purified recombinant enzyme, substrate L-methionine amide, pH 7.5, 30°C
0.9
-
purified recombinant enzyme, substrate L-methionine amide, pH 7.5, 30°C
1.5
-
purified recombinant enzyme, substrate L-leucine amide, pH 7.5, 30°C
1.8
purified recombinant enzyme, substrate L-leucine amide, pH 7.5, 30°C
105
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
107
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
1072
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
11
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
1225
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 8.0, 30°C
133
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
16
purified recombinant enzyme, substrate L-serine amide, pH 7.5, 30°C
16.7
purified recombinant enzyme, substrate L-alanine amide, pH 7.5, 30°C
17.5
-
purified recombinant enzyme, substrate L-alanine amide, pH 7.5, 30°C
182
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
20
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
21.6
-
purified recombinant enzyme, substrate L-serine amide, pH 7.5, 30°C
260
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
365
-
purified recombinant His-tagged enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
39
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
422
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
444
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 8.0, 30°C
47
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
5.3
-
crude recombinant enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C
520
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
68
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
94
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
0.1
purified recombinant enzyme, substrate L-phenylglycine, pH 7.5, 30°C
0.1
-
purified recombinant enzyme, substrate L-phenylglycine, pH 7.5, 30°C
443
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
443
purified recombinant enzyme, substrate L-aspartate, pH 7.5, 30°C
627
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
627
purified recombinant enzyme, substrate D-aspartate, pH 7.5, 30°C
63
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
63
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
681
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C
681
-
purified recombinant enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C
772
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C
772
-
purified recombinant enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C
additional information
-
300 U/liter culture
additional information
-
the effect of the concentration of L-alanine amide on the racemization reaction catalyzed by ACL racemase is investigated. Formation of D-alanine amide increases when the concentration of L-alanine amide is increased from 0.6 M to 1.2 M, indicating that the enzyme activity is not inhibited by the high substrate concentration
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ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
gene ABI14443, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene ACLR or Oant_4493, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene ACLR or Smed_5339, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene ACLR, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene JNB_04915, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene Mesop_2670, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene Mvan_2918, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene SM0020_01805, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene SMc02413, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
-
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
-
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Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Mechanism of alpha-amino-epsilon-caprolactam racemase reaction
Biochemistry
25
385-388
1986
Achromobacter obae
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
L-alpha-Amino-beta-thio-epsilon-caprolactam, a new sulfur-containing substrate for alpha-amino-epsilon-caprolactam racemase
FEBS Lett.
174
76-79
1984
Achromobacter obae
-
brenda
Ahmed, S.A.; Esaki, N.; Soda, K.
Purification and properties of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
FEBS Lett.
150
370-374
1982
Achromobacter obae, Achromobacter obae FERM-P776
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Mechanism of inactivation of alpha-amino-epsilon-caprolactam racemase by alpha-amino-delta-valerolactam
Agric. Biol. Chem.
49
2991-2997
1985
Achromobacter obae
-
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Properties of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Agric. Biol. Chem.
47
1887-1893
1983
Achromobacter obae
-
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Racemization of alpha-amino-delta-valerolactam catalyzed by alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Agric. Biol. Chem.
47
1149-1150
1983
Achromobacter obae
-
brenda
Fukumura, T.
Partial purification and some properties of alpha-amino-epsilon-caprolactam-racemizing enzyme from Achromobacter obae
Agric. Biol. Chem.
41
1509-1510
1977
Achromobacter obae
-
brenda
Plhackova, K.; Vojtisek, V.; Plachy, J.
Enzymic synthesis of L-lysine from DL-alpha-amino-epsilon-caprolactam by new microbial strains
Folia Microbiol. (Praha)
27
382-389
1982
Pseudomonas sp., Pseudomonas sp. CCM 3443
brenda
Crosby, J.
Synthesis of optically active compounds: A large scale perspective
Tetrahedron
47
4789-4846
1991
Achromobacter obae
-
brenda
Asano, Y.; Yamaguchi, S.
Dynamic kinetic resolution of amino acid amide catalyzed by D-aminopeptidase and alpha-amino-epsilon-caprolactam racemase
J. Am. Chem. Soc.
127
7696-7697
2005
Achromobacter obae
brenda
Yamaguchi, S.; Komeda, H.; Asano, Y.
New enzymatic method of chiral amino acid synthesis by dynamic kinetic resolution of amino acid amides: use of stereoselective amino acid amidases in the presence of alpha-amino-epsilon-caprolactam racemase
Appl. Environ. Microbiol.
73
5370-5373
2007
Achromobacter obae
brenda
Okazaki, S.; Suzuki, A.; Mizushima, T.; Kawano, T.; Komeda, H.; Asano, Y.; Yamane, T.
The novel structure of a pyridoxal 5-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Biochemistry
48
941-950
2009
Achromobacter obae (Q7M181), Achromobacter obae
brenda
Payoungkiattikun, W.; Okazaki, S.; Nakano, S.; Ina, A.; H-Kittikun, A.; Asano, Y.
In silico identification for alpha-amino-epsilon-caprolactam racemases by using information on the structure and function relationship
Appl. Biochem. Biotechnol.
176
1303-1314
2015
Glutamicibacter nicotianae, Brucella anthropi, Brucella anthropi (A6X7I5), Citreicella sp. SE45, Mycolicibacterium vanbaalenii (A1T974), Janibacter sp. HTCC2649 (A3TM80), Sinorhizobium medicae (A6UKD1), Mesorhizobium opportunistum (F7Y223), Sinorhizobium meliloti (H0FT96), Sinorhizobium meliloti (Q92MM4), Achromobacter obae (Q7M181), Mesorhizobium opportunistum WSM 2075 (F7Y223), Sinorhizobium meliloti CCNWSX0020 (H0FT96), Sinorhizobium medicae WSM 419 (A6UKD1), Mycolicibacterium vanbaalenii PYR-1 (A1T974), Glutamicibacter nicotianae NCIMB 41126, Brucella anthropi IA / NCBIMB41129, Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 (A6X7I5)
brenda
Matsui, D.; Fuhshuku, K.I.; Nagamori, S.; Takata, M.; Asano, Y.
Isolation and characterization of racemase from Ensifer sp. 23-3 that acts on alpha-aminolactams and alpha-amino acid amides
J. Ind. Microbiol. Biotechnol.
44
1503-1510
2017
Ensifer sp. 23-3
brenda
Payoungkiattikun, W.; Okazaki, S.; Ina, A.; H-Kittikun, A.; Asano, Y.
Characterization of an alpha-amino-epsilon-caprolactam racemase with broad substrate specificity from Citreicella sp. SE45
J. Ind. Microbiol. Biotechnol.
44
677-685
2017
Citreicella sp. SE45, Achromobacter obae (Q7M181)
brenda