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2-oxoglutarate + L-ornithine
D-glutamate + L-glutamate
-
-
-
?
D-2,4-Diaminobutyrate
L-2,4-Diaminobutyrate
-
10% of the activity relative to D-Lys
-
?
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
D-arginine
L-arginine
78.1% activity compared to LL-diaminopimelate
-
-
r
D-Asp
L-Asp
-
6% of the activity relative to D-Gln
-
?
D-aspartate
L-aspartate
-
lower substrate affinity for D-aspartate compared to L-aspartate
-
-
?
D-ethionine
L-ethionine
11% activity, compared to D-Lys
-
-
?
D-Gln
L-Gln
-
D-Glu is the best substrate
-
?
D-homoarginine
L-homoarginine
6.2% activity, compared to D-Lys
-
-
?
D-homoserine
L-homoserine
high activity with 75% of the activity in the other direction
-
-
r
D-isoleucine
L-isoleucine
-
-
-
r
D-leucine
L-leucine
-
-
-
r
D-Lys
L-Lys
100% activity
-
-
?
D-lysine
L-lysine
93.5% activity compared to LL-diaminopimelate
-
-
r
D-methionine
L-methionine
D-norvaline
L-norvaline
6.5% activity, compared to D-Lys
-
-
?
D-phenylalanine
L-phenylalanine
-
-
-
r
D-serine
pyruvate + NH3
-
alpha,beta-elimination reaction
-
-
?
D-threonine
L-threonine
-
-
-
r
D-tryptophan
L-tryptophan
-
-
-
r
D-tyrosine
L-tyrosine
-
-
-
r
D-valine
L-valine
-
-
-
r
L-2-Aminobutyrate
D-2-Aminobutyrate
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
L-alanine amide
D-alanine amide
L-aminobutyrate
D-aminobutyrate
L-asparagine
D-asparagine
L-aspartate
D-aspartate
-
higher substrate affinity for L-aspartate compared to D-aspartate
-
-
?
L-Citrulline
D-Citrulline
L-Homoarginine
L-Homoarginine
L-Homocitrulline
D-Homocitrulline
L-Homocysteine
D-Homocysteine
-
55% of the activity relative to L-Lys
-
?
L-homoserine
D-homoserine
L-isoleucine
D-isoleucine
L-leucine amide
D-leucine amide
L-Methionine
D-Methionine
L-methionine amide
D-methionine amide
L-Norleucine
D-Norleucine
L-phenylalanine
D-phenylalanine
L-phenylalanine amide
D-phenylalanine amide
L-phenylglycine amide
D-phenylglycine amide
L-Selenohomocysteine
D-Selenohomocysteine
-
27% of the activity relative to L-Lys
-
?
L-serine
pyruvate + NH3
-
alpha,beta-elimination reaction
-
-
?
L-serine amide
D-serine amide
L-threonine
2-oxobutyrate + NH3
-
alpha,beta-elimination reaction
-
-
?
L-tryptophan
D-tryptophan
L-tyrosine amide
D-tyrosine amide
L-valine amide
D-valine amide
LL-diaminopimelate
meso-diaminopimelate
N-acetyl-D-alanine
N-acetyl-L-alanine
-
-
-
-
r
N-acetyl-D-asparagine
N-acetyl-L-asparagine
-
-
-
-
r
N-acetyl-D-methionine
N-acetyl-L-methionine
-
-
-
-
r
N-acetyl-D-phenylalanine
N-acetyl-L-phenylalanine
-
-
-
-
r
N-acetyl-D-tryptophan
N-acetyl-L-tryptophan
-
-
-
-
r
N-carbamoyl-L-methionine
N-carbamoyl-D-methionine
-
-
-
-
r
N-succinyl-L-alanine
N-succinyl-D-alanine
-
-
-
-
r
N-succinyl-L-Arg
N-succinyl-D-Arg
-
-
-
-
r
N-succinyl-L-Asn
N-succinyl-D-Asn
-
-
-
-
r
N-succinyl-L-Asp
N-succinyl-D-Asp
-
-
-
-
r
N-succinyl-L-Gln
N-succinyl-D-Gln
-
-
-
-
r
N-succinyl-L-Glu
N-succinyl-D-Glu
-
-
-
-
r
N-succinyl-L-His
N-succinyl-D-His
-
-
-
-
r
N-succinyl-L-Ile
N-succinyl-D-Ile
-
-
-
-
r
N-succinyl-L-Leu
N-succinyl-D-Leu
-
-
-
-
r
N-succinyl-L-Lys
N-succinyl-D-Lys
-
-
-
-
r
N-succinyl-L-Met
N-succinyl-D-Met
-
-
-
-
r
N-succinyl-L-phenylalanine
N-succinyl-D-phenylalanine
N-succinyl-L-Ser
N-succinyl-D-Ser
-
-
-
-
r
N-succinyl-L-Trp
N-succinyl-D-Trp
-
-
-
-
r
N-succinyl-L-Tyr
N-succinyl-D-Tyr
-
-
-
-
r
N-succinyl-L-Val
N-succinyl-D-Val
-
-
-
-
r
N6-Acetyl-L-Lys
N6-Acetyl-D-Lys
S-Methyl-L-Cys
S-Methyl-D-Cys
additional information
?
-
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
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
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-Ala
L-Ala
12% activity, compared to D-Lys
-
-
?
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
r
D-Arg
L-Arg
-
-
-
-
?
D-Arg
L-Arg
-
65% of the activity relative to L-Lys
-
-
?
D-Arg
L-Arg
-
60% of the activity relative to D-Lys
-
-
?
D-Arg
L-Arg
-
21% of the activity relative to D-Gln
-
-
?
D-Arg
L-Arg
-
80% of the activity relative to L-Lys
-
-
?
D-Arg
L-Arg
95% activity, compared to D-Lys
-
-
?
D-Leu
L-Leu
-
-
-
r
D-Leu
L-Leu
broad substrate specificity
-
-
?
D-Leu
L-Leu
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-Met
L-Met
-
-
-
-
r
D-Met
L-Met
12% activity, compared to D-Lys
-
-
?
D-Met
L-Met
broad substrate specificity
-
-
?
D-Met
L-Met
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-methionine
L-methionine
4.8% activity compared to L-homoserine
-
-
r
D-methionine
L-methionine
-
-
-
r
D-ornithine
L-ornithine
46.7% activity compared to LL-diaLinopimelate
-
-
r
D-ornithine
L-ornithine
42% activity, compared to D-Lys
-
-
?
D-Phe
L-Phe
-
1% of the velocity relative to D-Glu
-
?
D-Phe
L-Phe
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-Phe
L-Phe
Phe is the most preferred substrate among the amino acids, broad substrate specificity
-
-
?
D-Phe
L-Phe
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-Phe
L-Phe
Phe is the most preferred substrate among the amino acids, broad substrate specificity
-
-
?
D-serine
L-serine
-
similar substrate affinity for both L-serine and D-serine
-
-
?
D-serine
L-serine
-
-
-
-
r
D-serine
L-serine
-
racemization reaction
-
-
r
D-serine
L-serine
-
-
-
r
L-2-Aminobutyrate
D-2-Aminobutyrate
-
-
-
?
L-2-Aminobutyrate
D-2-Aminobutyrate
-
4.7% of the activity relative to D-Lys
-
-
?
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-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-Ala
D-Ala
-
-
-
?
L-Ala
D-Ala
-
6% of the activity relative to L-Lys
-
-
?
L-Ala
D-Ala
-
D-Ala, 15% of the activity relative to D-Gln
-
-
?
L-Ala
D-Ala
-
9% of the activity relative to D-Lys
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
25.9% activity compared to LL-diaminopimelate
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
0.9% activity compared to L-homoserine
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-alanine amide
D-alanine amide
-
-
-
r
L-aminobutyrate
D-aminobutyrate
4.0% activity compared to LL-diaminopimelate
-
-
r
L-aminobutyrate
D-aminobutyrate
4.6% activity compared to L-homoserine
-
-
r
L-arginine
D-arginine
90.5% activity compared to LL-diaminopimelate
-
-
r
L-arginine
D-arginine
-
-
-
r
L-arginine
D-arginine
-
-
-
-
r
L-arginine
D-arginine
-
-
-
-
r
L-Asn
D-Asn
-
9% of the activity relative to L-Lys
-
?
L-Asn
D-Asn
-
12% of the activity relative to L-Lys
-
-
?
L-asparagine
D-asparagine
10.3% activity compared to LL-diaminopimelate
-
-
r
L-asparagine
D-asparagine
4.9% activity compared to L-homoserine
-
-
r
L-asparagine
D-asparagine
-
-
-
r
L-asparagine
D-asparagine
-
-
-
-
r
L-Citrulline
D-Citrulline
-
30% of the activity relative to L-Lys
-
-
?
L-Citrulline
D-Citrulline
-
45% of the activity relative to L-Lys
-
-
?
L-Citrulline
D-Citrulline
-
16% of the activity relative to D-Lys
-
?
L-Ethionine
D-Ethionine
-
-
-
-
?
L-Ethionine
D-Ethionine
-
67% of the activity relative to L-Lys
-
-
?
L-Ethionine
D-Ethionine
-
-
-
?
L-Ethionine
D-Ethionine
-
83% of the activity relative to L-Lys
-
-
?
L-Ethionine
D-Ethionine
-
76% of the activity relative to D-Lys
-
-
?
L-Glu
D-Glu
-
-
-
-
?
L-Glu
D-Glu
-
57% of the activity relative to L-Lys
-
?
L-Glu
D-Glu
-
80% of the activity relative to L-Lys
-
-
?
L-Glu
D-Glu
-
no activity with D-Glu
-
-
?
L-glutamate
D-glutamate
-
-
-
r
L-glutamate
D-glutamate
-
-
-
r
L-glutamine
D-glutamine
14.4% activity compared to LL-diaminopimelate
-
-
r
L-glutamine
D-glutamine
0.7% activity compared to L-homoserine
-
-
r
L-glutamine
D-glutamine
-
-
-
r
L-His
D-His
-
6% of the activity relative to L-Lys
-
-
?
L-His
D-His
-
1.8% of the activity relative to D-Lys
-
?
L-histidine
D-histidine
32.1% activity compared to LL-diaminopimelate
-
-
r
L-histidine
D-histidine
7.9% activity compared to L-homoserine
-
-
r
L-histidine
D-histidine
-
-
-
r
L-Homoarginine
L-Homoarginine
-
67% of the activity relative to L-Lys
-
?
L-Homoarginine
L-Homoarginine
-
80% of the activity relative to L-Lys
-
?
L-Homocitrulline
D-Homocitrulline
-
34% of the activity relative to L-Lys
-
?
L-Homocitrulline
D-Homocitrulline
-
45% of the activity relative to L-Lys
-
-
?
L-homoserine
D-homoserine
-
12% of the activity relative to L-Lys
-
?
L-homoserine
D-homoserine
9.3% activity compared to LL-diaminopimelate
-
-
r
L-homoserine
D-homoserine
9.3% activity compared to LL-diaminopimelate
-
-
r
L-homoserine
D-homoserine
best substrate
-
-
r
L-homoserine
D-homoserine
best substrate
-
-
r
L-homoserine
D-homoserine
-
22% of the activity relative to L-Lys
-
-
?
L-isoleucine
D-isoleucine
3.9% activity compared to L-homoserine
-
-
r
L-isoleucine
D-isoleucine
-
-
-
r
L-Leu
D-Leu
-
12% of the activity relative to L-Lys
-
-
?
L-Leu
D-Leu
-
D-Leu, 13% of the activity relative to D-Gln
-
-
?
L-Leu
D-Leu
-
10% of the activity relative to L-Lys
-
-
?
L-Leu
D-Leu
-
3% of the activity relative to D-Lys
-
-
?
L-leucine
D-leucine
6.6% activity compared to L-homoserine
-
-
r
L-leucine
D-leucine
-
-
-
r
L-leucine
D-leucine
-
-
-
r
L-leucine amide
D-leucine amide
-
-
-
r
L-leucine amide
D-leucine amide
-
-
-
-
r
L-leucine amide
D-leucine amide
-
-
-
-
r
L-leucine amide
D-leucine amide
-
-
-
r
L-leucine amide
D-leucine amide
-
-
-
r
L-Lys
D-Lys
-
-
-
-
?
L-Lys
D-Lys
-
D-Lys at 22% of the activity relative to D-Gln
-
-
?
L-lysine
D-lysine
81.2% activity compared to LL-diaminopimelate
-
-
r
L-lysine
D-lysine
-
-
-
-
r
L-lysine
D-lysine
-
-
-
-
r
L-lysine
D-lysine
-
-
-
r
L-lysine
D-lysine
-
-
-
-
r
L-lysine
D-lysine
-
-
-
-
r
L-Met
D-Met
-
-
-
-
?
L-Met
D-Met
-
67% of the activity relative to L-Lys
-
-
?
L-Met
D-Met
-
D-Met, 42% of the activity relative to D-Gln
-
-
?
L-Met
D-Met
-
66% of the activity relative to L-Lys
-
-
?
L-Met
D-Met
-
48% of the activity relative to D-Lys
-
-
?
L-Methionine
D-Methionine
13.1% activity compared to LL-diaminopimelate
-
-
r
L-Methionine
D-Methionine
6.0% activity compared to L-homoserine
-
-
r
L-Methionine
D-Methionine
7.9% activity compared to L-homoserine
-
-
r
L-Methionine
D-Methionine
6.0% activity compared to L-homoserine
-
-
r
L-Methionine
D-Methionine
-
-
-
r
L-Methionine
D-Methionine
-
-
-
r
L-Methionine
D-Methionine
-
-
-
-
r
L-Methionine
D-Methionine
-
-
-
-
r
L-Methionine
D-Methionine
-
-
-
r
L-Methionine
D-Methionine
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-methionine amide
D-methionine amide
-
-
-
r
L-Norleucine
D-Norleucine
-
28% of the activity relative to L-Lys
-
-
?
L-Norleucine
D-Norleucine
5.6% activity compared to LL-diaminopimelate
-
-
r
L-Norleucine
D-Norleucine
5.6% activity compared to LL-diaminopimelate
-
-
r
L-Norleucine
D-Norleucine
1.2% activity compared to L-homoserine
-
-
r
L-Norleucine
D-Norleucine
1.2% activity compared to L-homoserine
-
-
r
L-Norleucine
D-Norleucine
-
-
-
?
L-Norleucine
D-Norleucine
-
45% of the activity relative to L-Lys
-
-
?
L-Norvaline
D-Norvaline
3.6% activity compared to LL-diaminopimelate
-
-
r
L-Norvaline
D-Norvaline
3.6% activity compared to LL-diaminopimelate
-
-
r
L-Norvaline
D-Norvaline
5.8% activity compared to L-homoserine
-
-
r
L-Norvaline
D-Norvaline
5.8% activity compared to L-homoserine
-
-
r
L-Norvaline
D-Norvaline
-
-
-
?
L-Orn
D-Orn
-
-
-
-
?
L-Orn
D-Orn
-
79% of the activity relative to L-Lys
-
?
L-Orn
D-Orn
-
80% of the activity relative to L-Lys
-
-
?
L-Ornithine
D-Ornithine
86.2% activity compared to LL-diaminopimelate
-
-
r
L-Ornithine
D-Ornithine
86.2% activity compared to LL-diaminopimelate
-
-
r
L-phenylalanine
D-phenylalanine
21.9% activity compared to LL-diaminopimelate
-
-
r
L-phenylalanine
D-phenylalanine
0.6% activity compared to L-homoserine
-
-
r
L-phenylalanine
D-phenylalanine
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
r
L-phenylalanine amide
D-phenylalanine amide
-
-
-
r
L-phenylalanine amide
D-phenylalanine 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-phenylglycine amide
D-phenylglycine amide
-
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
r
L-phenylglycine amide
D-phenylglycine amide
-
-
-
r
L-Ser
D-Ser
-
10% of the activity relative to L-Lys
-
-
?
L-Ser
D-Ser
-
8.7% of the activity relative to D-Lys
-
?
L-Ser
D-Ser
-
D-Ser, 31% of the activity relative to D-Gln
-
-
?
L-serine
D-serine
-
similar substrate affinity for both L-serine and D-serine
-
-
?
L-serine
D-serine
19.1% activity compared to LL-diaminopimelate
-
-
r
L-serine
D-serine
1.5% activity compared to L-homoserine
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
racemization reaction
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-serine amide
D-serine amide
-
-
-
-
r
L-serine amide
D-serine amide
-
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-serine amide
D-serine amide
-
-
-
r
L-Thr
L-Thr
-
no activity
-
-
?
L-Thr
L-Thr
-
3% of the activity relative to L-Lys
-
?
L-threonine
D-threonine
-
-
-
r
L-threonine
D-threonine
-
-
-
r
L-Trp
D-Trp
-
-
-
-
r
L-tryptophan
D-tryptophan
-
-
-
r
L-tryptophan
D-tryptophan
-
-
-
r
L-tyrosine
D-tyrosine
22.8% activity compared to LL-diaminopimelate
-
-
r
L-tyrosine
D-tyrosine
-
-
-
r
L-tyrosine amide
D-tyrosine amide
-
-
-
r
L-tyrosine amide
D-tyrosine amide
-
-
-
-
r
L-tyrosine amide
D-tyrosine amide
-
-
-
r
L-tyrosine amide
D-tyrosine amide
-
-
-
r
L-tyrosine amide
D-tyrosine amide
-
-
-
r
L-valine
D-valine
6.2% activity compared to L-homoserine
-
-
r
L-valine
D-valine
-
-
-
r
L-valine
D-valine
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
-
r
L-valine amide
D-valine amide
-
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
L-valine amide
D-valine amide
-
-
-
r
LL-diaminopimelate
meso-diaminopimelate
best substrate
-
-
r
LL-diaminopimelate
meso-diaminopimelate
0.7% activity compared to L-homoserine
-
-
r
N-succinyl-L-phenylalanine
N-succinyl-D-phenylalanine
-
-
-
-
?
N-succinyl-L-phenylalanine
N-succinyl-D-phenylalanine
-
-
-
-
r
N6-Acetyl-L-Lys
N6-Acetyl-D-Lys
-
37% of the activity relative to L-Lys
-
?
N6-Acetyl-L-Lys
N6-Acetyl-D-Lys
-
80% of the activity relative to L-Lys
-
-
?
S-Methyl-L-Cys
S-Methyl-D-Cys
-
43% of the activity relative to L-Lys
-
?
S-Methyl-L-Cys
S-Methyl-D-Cys
-
3% of the activity relative to L-Lys
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
-
DAR1 has no detectable activity with 100 mM L-glutamate or 100 mM L-alanine
-
-
?
additional information
?
-
enzyme RacX displays broad substrate specificity but low catalytic activity. RacX preferentially racemizes arginine, lysine, and ornithine. Histochemic product analysis and quantification by HPLC and spectroscopy
-
-
?
additional information
?
-
enzyme RacX displays broad substrate specificity but low catalytic activity. RacX preferentially racemizes arginine, lysine, and ornithine. Histochemic product analysis and quantification by HPLC and spectroscopy
-
-
?
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 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 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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
enzyme YgeA displays broad substrate specificity but low catalytic activity. YgeA preferentially catalyzes the racemization of homoserine. Histochemic product analysis and quantification by HPLC and spectroscopy
-
-
?
additional information
?
-
enzyme YgeA displays broad substrate specificity but low catalytic activity. YgeA preferentially catalyzes the racemization of homoserine. Histochemic product analysis and quantification by HPLC and spectroscopy
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site
-
-
?
additional information
?
-
enzyme Ls-MalY shows cystathionine beta-lyase (EC 4.4.1.8) and amino acid racemase activity with various amino acids, such as Ala, Arg, Asn, Glu, Gln, His, Leu, Lys, Met, Ser, Thr, Trp, and Val, substrate specificity, overview. L-Tyr and D-Tyr are poor substrates. Thr is only converted from L- to D-Thr, but not vice versa. The epsilon-amino group of Lys233 in the primary structure of Ls-MalY likely bound to pyridoxal 5'-phosphate, and Lys233 is an essential residue for Ls-MalY to catalyze both the amino acid racemase and beta-lyase reactions. Tyr123 is a catalytic residue in the amino acid racemase reaction but strongly affects beta-lyase activity
-
-
?
additional information
?
-
Ls-MalY is a bifunctional amino acid racemase with multiple substrate specificity, both the amino acid racemase and beta-lyase reactions of Ls-MalY are catalyzed at the same active site
-
-
?
additional information
?
-
enzyme Ls-MalY shows cystathionine beta-lyase (EC 4.4.1.8) and amino acid racemase activity with various amino acids, such as Ala, Arg, Asn, Glu, Gln, His, Leu, Lys, Met, Ser, Thr, Trp, and Val, substrate specificity, overview. L-Tyr and D-Tyr are poor substrates. Thr is only converted from L- to D-Thr, but not vice versa. The epsilon-amino group of Lys233 in the primary structure of Ls-MalY likely bound to pyridoxal 5'-phosphate, and Lys233 is an essential residue for Ls-MalY to catalyze both the amino acid racemase and beta-lyase reactions. Tyr123 is a catalytic residue in the amino acid racemase reaction but strongly affects beta-lyase activity
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
-
racemization and elimination activities reside at the same active site of enzyme. Racemization activity is specific to serine, elimination activity has a broader specificity for L-amino acids with a suitable leaving group at the beta-carbon
-
-
?
additional information
?
-
-
ration of elimination reaction/racemization reaction for substrate L-serine is 3.7
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
-
catalyzes nonstereospecific transamination: production of D-Glu and L-Glu from 2-oxoglutarate through transamination with L-Orn
-
-
?
additional information
?
-
-
the relative activity is 1 for Leu, 1.8 for L-2-aminobutyrate, 3.3 for L-Ala, 5.2 for norvaline, 5.9 for L-norleucine, 7.5 for D-Arg, 10.6 for L-Met, 13.2 for D-Lys, and 15.9 for L-ethionine
-
-
?
additional information
?
-
-
no activity with: D-Glu, L-Ile, L-Phe, L-Thr, L-Val
-
-
?
additional information
?
-
no activity with Pro, Asp or Glu
-
-
?
additional information
?
-
-
no activity with Pro, Asp or Glu
-
-
?
additional information
?
-
the enzyme predominantly shows activity toward hydrophobic and aromatic amino acids. No activity toward Arg, His, Gln, and Asn
-
-
?
additional information
?
-
PH0138 gene encodes an amino acid racemase, AAR. No activity with L-Pro, D-Asp, and D-Glu
-
-
?
additional information
?
-
-
PH0138 gene encodes an amino acid racemase, AAR. No activity with L-Pro, D-Asp, and D-Glu
-
-
?
additional information
?
-
the enzyme BAR has broad substrate specificity, it is active toward Met, Leu, Phe, Ile, Val, Ala, Trp, Tyr, Thr, and Ser, but no activity toward Pro, Asp, Glu, Arg, His, Gln, Cys, Lys, and Asn. In particular, the high reaction rate with Trp and Tyr, in addition to Leu, Met and Phe as substrates is a noteworthy feature of this enzyme. Histochemic analysis of D- and L-amino acid products. The Vmax values obtained with Ala, Val, Ile, Leu, and Met in D-amino acid forming reactions are lower than in L-amino acid forming reactions. By contrast, the Vmax values for Phe, Tyr, and Trp in D-amino acid forming reactions are higher than in L-amino acid forming reaction. The D-forms of Arg, His, Asn, and Gln are not quantitatively detected
-
-
?
additional information
?
-
no activity with Pro, Asp or Glu
-
-
?
additional information
?
-
PH0138 gene encodes an amino acid racemase, AAR. No activity with L-Pro, D-Asp, and D-Glu
-
-
?
additional information
?
-
the enzyme predominantly shows activity toward hydrophobic and aromatic amino acids. No activity toward Arg, His, Gln, and Asn
-
-
?
additional information
?
-
the enzyme BAR has broad substrate specificity, it is active toward Met, Leu, Phe, Ile, Val, Ala, Trp, Tyr, Thr, and Ser, but no activity toward Pro, Asp, Glu, Arg, His, Gln, Cys, Lys, and Asn. In particular, the high reaction rate with Trp and Tyr, in addition to Leu, Met and Phe as substrates is a noteworthy feature of this enzyme. Histochemic analysis of D- and L-amino acid products. The Vmax values obtained with Ala, Val, Ile, Leu, and Met in D-amino acid forming reactions are lower than in L-amino acid forming reactions. By contrast, the Vmax values for Phe, Tyr, and Trp in D-amino acid forming reactions are higher than in L-amino acid forming reaction. The D-forms of Arg, His, Asn, and Gln are not quantitatively detected
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
additional information
?
-
the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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 is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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
-
-
?
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94
D-Aspartate
-
in 50 mM Tris-HCl buffer, pH 8.0, at 30°C
25.1
D-homoserine
pH 8.5, 37°C, recombinant enzyme
9.54
D-isoleucine
pH 7.0, 80°C, recombinant enzyme
4.19
D-leucine
pH 7.0, 80°C, recombinant enzyme
69.3
D-Lysine
pH 8.5, 37°C, recombinant enzyme
2.78
D-phenylalanine
pH 7.0, 80°C, recombinant enzyme
1.68
D-tryptophan
pH 7.0, 80°C, recombinant enzyme
2.77
D-tyrosine
pH 7.0, 80°C, recombinant enzyme
9.82
D-valine
pH 7.0, 80°C, recombinant enzyme
8
L-aspartate
-
in 50 mM Tris-HCl buffer, pH 8.0, at 30°C
171
L-homoserine
pH 8.5, 37°C, recombinant enzyme
3.94
L-isoleucine
pH 7.0, 80°C, recombinant enzyme
4.95
L-leucine
pH 7.0, 80°C, recombinant enzyme
27.9
L-lysine
pH 8.5, 37°C, recombinant enzyme
8.23
L-phenylalanine
pH 7.0, 80°C, recombinant enzyme
5.84
L-tryptophan
pH 7.0, 80°C, recombinant enzyme
2.23
L-tyrosine
pH 7.0, 80°C, recombinant enzyme
3.41
L-valine
pH 7.0, 80°C, recombinant enzyme
17
N-acetyl-D-alanine
-
-
18
N-acetyl-D-asparagine
-
-
7
N-acetyl-D-methionine
-
-
2 - 3
N-acetyl-D-phenylalanine
-
-
2
N-acetyl-D-tryptophan
-
-
41
N-acetyl-L-alanine
-
-
27
N-acetyl-L-asparagine
-
-
8
N-acetyl-L-methionine
-
-
43
N-acetyl-L-phenylalanine
-
-
2
N-acetyl-L-tryptophan
-
-
2
N-carbamoyl-D-methionine
-
-
5
N-carbamoyl-L-methionine
-
-
0.13
N-succinyl-D-alanine
-
-
0.04
N-succinyl-D-phenylalanine
-
-
0.12
N-succinyl-L-alanine
-
-
0.13
N-succinyl-L-phenylalanine
-
-
additional information
additional information
-
7.4
D-Ala
-
-
35.6
D-alanine
pH 7.0, 80°C, recombinant enzyme
150
D-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
18
D-Asn
-
pure lyophilisates, 20°C, pH 7, Vmax: 770 micromol/min/g
50
D-Asn
-
pure lyophilisates, 25°C, pH 7, Vmax: 1299 micromol/min/g
62
D-Asn
-
pure lyophilisates, 30°C, pH 7, Vmax: 1881 micromol/min/g
66
D-Asn
-
pure lyophilisates, 35°C, pH 7, Vmax: 2585 micromol/min/g
103
D-Asn
-
pure lyophilisates, 40°C, pH 7, Vmax: 4032 micromol/min/g
0.42
D-Lys
-
-
1.6
D-Met
-
-
2 - 3
D-Met
-
crude lyophilisates, 30°C, pH 7, Vmax: 2075 micromol/min/g
22
D-Met
-
crude lyophilisates, 25°C, pH 7, Vmax: 1892 micromol/min/g
25
D-Met
-
crude lyophilisates, 20°C, pH 7, Vmax: 1696 micromol/min/g
28
D-Met
-
crude lyophilisates, 25°C, pH 8, Vmax: 3627 micromol/min/g
30
D-Met
-
crude lyophilisates, 35°C, pH 7, Vmax: 2512 micromol/min/g
32
D-Met
-
crude lyophilisates, 40°C, pH 7, Vmax: 2668 micromol/min/g
42
D-Met
-
crude lyophilisates, 25°C, pH 6, Vmax: 1160 micromol/min/g
4.8
D-methionine
-
100% aqueous
7.86
D-methionine
pH 7.0, 80°C, recombinant enzyme
9
D-methionine
-
10% methanol
11.1
D-methionine
-
10% acetonitril
11.9
D-methionine
-
40% acetonitril
13.2
D-methionine
-
20% acetonitril
15.8
D-methionine
-
20% methanol
24.3
D-methionine
-
40% methanol
2.78
D-Phe
pH 7.0, 80°C
1
D-Ser
-
-
14.5
D-serine
-
pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction
49
D-serine
-
pH 8.0, 37°C, racemization reaction
36
L-2-aminobutyrate
-
-
36
L-2-aminobutyrate
-
L-Ala
7
L-Ala
-
-
56
L-alanine
pH 7.0, 80°C, recombinant enzyme
169
L-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
30
L-Asn
-
pure lyophilisates, 20°C, pH 7, Vmax: 1626 micromol/min/g
47
L-Asn
-
pure lyophilisates, 25°C, pH 7, Vmax: 2427 micromol/min/g
76
L-Asn
-
pure lyophilisates, 30°C, pH 7, Vmax: 3930 micromol/min/g
101
L-Asn
-
pure lyophilisates, 35°C, pH 7, Vmax: 5683 micromol/min/g
4.95
L-Leu
pH 7.0, 80°C
33
L-Leu
-
L-2-aminobutyrate
0.55
L-Lys
-
-
1.2
L-Met
-
-
2 - 3
L-Met
-
crude lyophilisates, 25°C, pH 7, Vmax: 2150 micromol/min/g
20
L-Met
-
crude lyophilisates, 25°C, pH 8, Vmax: 2951 micromol/min/g
30
L-Met
-
crude lyophilisates, 25°C, pH 6, Vmax: 1174 micromol/min/g
30
L-Met
-
crude lyophilisates, 30°C, pH 7, Vmax: 2296 micromol/min/g
31
L-Met
-
crude lyophilisates, 20°C, pH 7, Vmax: 1889 micromol/min/g
35
L-Met
-
crude lyophilisates, 40°C, pH 7, Vmax: 2847 micromol/min/g
39
L-Met
-
crude lyophilisates, 35°C, pH 7, Vmax: 2833 micromol/min/g
4.1
L-methionine
-
100% aqueous
4.28
L-methionine
pH 7.0, 80°C, recombinant enzyme
7.8
L-methionine
-
10% methanol
9.4
L-methionine
-
20% methanol
11.5
L-methionine
-
10% acetonitril
13.2
L-methionine
-
20% acetonitril
16.1
L-methionine
-
40% acetonitril
22.3
L-methionine
-
40% methanol
0.9
L-Orn
-
-
3.8
L-serine
-
pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction
15
L-serine
-
in 50 mM Tris-HCl buffer, pH 8.5, for Ser reactions, at 30°C
16
L-serine
-
in 50 mM Tris-HCl buffer, pH 8.5, for Ser reactions, at 30°C
30
L-serine
-
pH 8.0, 37°C, racemization reaction
additional information
additional information
-
model-based calculations suggested that a methanol content of 10% and an acetonitrile content of 20% provide maximum productivity in enzyme membrane reactor (EMR) operations. However product concentrations are decreased in comparison to purely aqueous operation due to decreasing solubility of methionine with increasing organic solvent content.
-
additional information
additional information
-
no activity with N-Succinyl-L-Pro
-
additional information
additional information
kinetics, Hanes-Woolf plots
-
additional information
additional information
kinetics, Hanes-Woolf plots
-
additional information
N-Succinyl-L-Arg
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Asn
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Asp
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Cys
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Gln
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Glu
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Lys
-
low specific rotation prevented kinetic analysis
additional information
N-Succinyl-L-Thr
-
low specific rotation prevented kinetic analysis
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0.00588
-
substrate Trp, wildtype BAR
0.00706
-
substrate Phe, mutant Y396C
0.00782
-
substrate Ala, wildtype BAR
0.00838
-
substrate Phe, wildtype BAR
0.0121
-
substrate Ala, mutant I83L, D361V, Y396C
0.0141
-
substrate Ala, mutant Y293A, Y301S, Y396C
0.0144
-
substrate Ala, mutant L126H, Y396C
0.0249
-
substrate Phe, mutant Y293A, Y301S, Y396C
0.0257
-
substrate Phe, mutant I83L, D361V, Y396C
0.026
-
substrate Ala, mutant I384M
0.0267
-
substrate Trp, mutant Y293A, Y301S, Y396C
0.0303
-
substrate Trp, mutant I83L, D361V, Y396C
0.03215
-
substrate Lys, mutant Y396C
0.0436
-
substrate Phe, mutant L126H, Y396C
0.0487
-
substrate Trp, mutant Y396C
0.0524
-
substrate Trp, mutant L126H, Y396C
0.0744
-
substrate Phe, mutant I384M
0.1
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-serine
0.124
-
substrate Trp, mutant I384M
0.132
-
substrate Lys, wildtype BAR
0.15
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-asparagine
0.223
-
substrate Lys, mutant I384M
0.3
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-serine
0.36
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-methionine
0.458
-
substrate Lys, mutant Y293A, Y301S, Y396C
0.473
-
substrate Lys, mutant I83L, D361V, Y396C
0.477
-
substrate Lys, mutant L126H, Y396C
0.62
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-arginine
0.64
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-lysine
0.82
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-asparagine
0.825
-
substrate Ala, mutant Y396C
10.5
substrate: D-Met, pH 8.0, 80°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
1224
-
purified recombinant wild-type enzyme, pH 7.0, 37°C, substrate L-arginine
1225
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 8.0, 30°C
1250
-
L-Lys as substrate
133
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
1423
-
purified recombinant wild-type enzyme, pH 7.0, 37°C, substrate L-lysine
15.6
substrate: D-Leu, pH 8.0, 80°C
182
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
2
substrate: D-Ala, pH 8.0, 80°C
2.46
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-lysine
20
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
209
-
purified recombinant wild-type enzyme, pH 7.0, 37°C, substrate L-serine
22.7
substrate: D-Phe, pH 8.0, 80°C
256
-
purified recombinant wild-type enzyme, pH 7.0, 37°C, substrate L-methionine
260
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
3.22
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-arginine
3.9
substrate: D-Val, pH 8.0, 80°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
443
purified enzyme, substrate L-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
520
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
56
-
purified recombinant wild-type enzyme, pH 7.0, 37°C, substrate L-alanine
627
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
68
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
7.5
-
purified recombinant wild-type enzyme, pH 7.0, 37°C, substrate L-asparagine
772
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C
94
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
additional information
-
wildtype BAR, specific activity for L-Lys 100%, L-Arg 65%, L-Ala 33%, L-Ser 20%, L-Met 14%, L-Cys 14%, L-Leu 3.3%, L-His 1.6%, L-Phe 0.29%, L-Pro 0.1.3%, L-Thr 0.069%, L-Asn 0.054%, L-Asp 0.01%, L-Trp 0.006%, L-Val 0.003%
0.12
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-alanine
0.12
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-methionine
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
708.4
-
-
708.4
-
L-Met as substrate
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Soda, K.; Osumi, T.
Crystalline amino acid racemase with low substrate specificity
Biochem. Biophys. Res. Commun.
35
363-368
1969
Pseudomonas putida
brenda
Soda, K.; Osumi, T.
Amino acid racemase (Pseudomonas striata)
Methods Enzymol.
17
629-636
1971
Pseudomonas putida
-
brenda
Kimura, T.; Esaki, N.; Tanaka, H.; Soda, K.
Inactivation of amino acid racemase by S-(N-methylthiocarbamoyl)-D,L-cysteine
Agric. Biol. Chem.
48
383-388
1984
Pseudomonas putida
-
brenda
Roise, D.; Soda, K.; Yagi, T.; Walsh, C.T.
Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of beta-substituted alanines: kinetics, stoichiometry, active site peptide, and mechanistic studies
Biochemistry
23
5195-5201
1984
Pseudomonas putida
brenda
Badet, B.; Floss, H.G.; Walsh, C.T.
Stereochemical studies of processing of D- and L-isomers of suicide substrates by an amino acid racemase from Pseudomonas striata
J. Chem. Soc. Chem. Commun.
1984
838-840
1984
Pseudomonas putida
-
brenda
Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.
Purification and characterization of amino acid racemase with very broad substrate specificity from Aeromonas caviae
Agric. Biol. Chem.
51
173-180
1987
Aeromonas caviae
-
brenda
Shen, S.j.; Floss, H.G.; Kumagai, H.; Yamada, H.; Esaki, N.; Soda, K.; Wasserman, S.A.; Walsh, C.
Mechanism of pyridoxal phosphate-dependent enzymatic amino-acid racemization
J. Chem. Soc. Chem. Commun.
1983
82-83
1983
Pseudomonas putida
-
brenda
Lim, Y.H.; Yokoigawa, K.; Esaki, N.; Soda, K.
A new amino acid racemase with threonine alpha-epimerase activity from Pseudomonas putida: purification and characterization
J. Bacteriol.
175
4213-4217
1993
Pseudomonas putida
brenda
Lim, Y.H.; Yoshimura, T.; Kurokawa, Y.; Esaki, N.; Soda, K.
Nonstereospecific transamination catalyzed by pyridoxal phosphate-dependent amino acid racemases of broad substrate specificity
J. Biol. Chem.
273
4001-4005
1988
Pseudomonas putida
brenda
Asano, Y.; Endo, K.
Amino acid racemase with broad substrate specificity, its properties and use in phenylalanine racemization
Appl. Microbiol. Biotechnol.
29
523-527
1988
Pseudomonas putida
-
brenda
Ishiwata, K.I.; Fukuhara, N.; Shimada, M.; Makiguchi, N.; Soda, K.
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