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Information on EC 5.1.1.10 - amino-acid racemase
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5.1.1.10 amino-acid racemaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 5.1.1.10
-
racemization
- pyridoxal
- synthesis
-
plp-dependent
-
alpha-hydrogen
-
plp-binding
- buchneri
-
5'-phosphate-dependent
-
2-epimerase
- biotechnology
- diagnostics
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
amino acid racemase, acl racemase, broad-spectrum amino acid racemase, broad specificity amino acid racemase, amino-acid racemase, broad-specificity amino acid racemase, broad substrate specificity amino acid racemase, gknsaar, n-succinylamino acid racemase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAR
ACL racemase
amino acid racemase
BAR
broad substrate specificity amino acid racemase
broad-specificity amino acid racemase
broad-spectrum amino acid racemase
Bsar
L-Amino acid racemase
-
-
-
-
LACBS_00576
MalY
patB
PH0138
PLP-independent amino acid racemase
Racemase, amino acid
-
-
-
-
RacX
YgeA
additional information
additional information
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
cf. EC 5.1.1.15
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an L-amino acid = a D-amino acid
the results of the mechanistic studies argue against a single base mechanism and are best rationalized in terms of a double base model where only one of the bases undergoes proton exchange with the solvent while the amino acid is enzyme-bound
-
an L-amino acid = a D-amino acid
the results of the mechanistic studies argue against a single base mechanism and are best rationalized in terms of a double base model where only one of the bases undergoes proton exchange with the solvent while the amino acid is enzyme-bound
-
an L-amino acid = a D-amino acid
enzyme abstracts a hydrogen nonstereospecifically from C-4' of the coenzyme
-
an L-amino acid = a D-amino acid
significant internal return of the alpha-hydrogen
-
an L-amino acid = a D-amino acid
the racemization of ACL racemase proceeds via a two-base mechanism
an L-amino acid = a D-amino acid
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
amino-acid racemase
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
9068-61-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-2,4-Diaminobutyrate
L-2,4-Diaminobutyrate
-
10% of the activity relative to D-Lys
-
?
D-arginine
L-arginine
78.1% activity compared to LL-diaminopimelate
-
-
r
D-aspartate
L-aspartate
-
lower substrate affinity for D-aspartate compared to L-aspartate
-
-
?
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-lysine
L-lysine
93.5% activity compared to LL-diaminopimelate
-
-
r
L-aspartate
D-aspartate
-
higher substrate affinity for L-aspartate compared to D-aspartate
-
-
?
L-Homocysteine
D-Homocysteine
-
55% of the activity relative to L-Lys
-
?
L-Selenohomocysteine
D-Selenohomocysteine
-
27% of the activity relative to L-Lys
-
?
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
-
-
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-Leu
L-Leu
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
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-ornithine
L-ornithine
46.7% activity compared to LL-diaLinopimelate
-
-
r
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
-
-
?
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-alanine
D-alanine
25.9% activity compared to LL-diaminopimelate
-
-
r
L-alanine
D-alanine
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
-
-
r
L-alanine amide
D-alanine amide
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
-
-
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-asparagine
D-asparagine
10.3% activity compared to LL-diaminopimelate
-
-
r
L-asparagine
D-asparagine
4.9% activity compared to L-homoserine
-
-
r
L-glutamine
D-glutamine
14.4% activity compared to LL-diaminopimelate
-
-
r
L-histidine
D-histidine
32.1% activity compared to LL-diaminopimelate
-
-
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
9.3% activity compared to LL-diaminopimelate
-
-
r
L-homoserine
D-homoserine
9.3% activity compared to LL-diaminopimelate
-
-
r
L-isoleucine
D-isoleucine
3.9% activity compared to L-homoserine
-
-
r
L-lysine
D-lysine
81.2% activity compared to LL-diaminopimelate
-
-
r
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
Escherichia coli K-12 / MG1655
6.0% activity compared to L-homoserine
-
-
r
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
Escherichia coli K-12 / MG1655
1.2% activity compared to L-homoserine
-
-
r
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-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-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-tyrosine
D-tyrosine
22.8% activity compared to LL-diaminopimelate
-
-
r
LL-diaminopimelate
meso-diaminopimelate
0.7% activity compared to L-homoserine
-
-
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
-
?
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
?
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
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
?
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
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
?
-
Brucella anthropi IA / NCBIMB41129
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
?
-
Brucella anthropi IA / NCBIMB41129
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
?
-
Escherichia coli K-12 / MG1655
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
?
-
Glutamicibacter nicotianae NCIMB 41126
-
the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
Glutamicibacter nicotianae NCIMB 41126
-
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
?
-
Latilactobacillus sakei LT-13
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
?
-
Latilactobacillus sakei LT-13
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Leu
L-Leu
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-Met
L-Met
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-Phe
L-Phe
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
D-Phe
L-Phe
the enzyme is likely responsible for utilization of d-amino acids for growth
-
-
?
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
?
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
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
?
-
Brucella anthropi IA / NCBIMB41129
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 CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
?
additional information
?
-
Glutamicibacter nicotianae NCIMB 41126
-
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
?
-
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
?
-
Latilactobacillus sakei LT-13
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
?
-
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 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 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 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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
holoenzyme contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
holoenzyme contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of subunit
pyridoxal 5'-phosphate
activity is dependent on. In the absence of pyridoxal 5'-phosphate (about 10%) the activity of the purified recombinant enzyme is still remaining and is fully restored by the addition of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
PLP, the enzyme is a fold-type I PLP-dependent enzyme
additional information
pyridoxal 5'-phosphate is not required by the enzyme
-
additional information
pyridoxal 5'-phosphate is not required by the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Co2+
-
enzyme requires a divalent cation for activity. Maximal enzymatic activity with Co2+
Mg2+
-
MgCl2 alone (2 mM) has only a small effect on enzyme racemase activity, but when Mg2+ and ATP are present, the enzyme shows the largest activity for the D-Asp and D-Ser conversions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-chloroalanine
-
inactivator binds to the same Lys residue which binds pyridoxyl 5'-phosphate
3-Fluoroalanine
-
inactivator binds to the same Lys residue which binds pyridoxyl 5'-phosphate
ATP
-
inhibitory to L-serine O-sulfate dehydration reaction, activating for racemization reraction
O-acetylserine
-
inactivator binds to the same Lys residue which binds pyridoxyl 5'-phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
ATP alone (4 mM) significantly increases enzyme activity, but when the combination of ATP and Mg2+ is present, the enzyme shows the largest activity for the D-Asp and D-Ser conversions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
150
D-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
169
L-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1830
D-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
2310
L-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
additional information
additional information
-
N-Succinyl-L-Cys, low specific rotation prevented kinetic analysis
-
additional information
additional information
-
N-Succinyl-L-Thr, low specific rotation prevented kinetic analysis
-
additional information
additional information
-
no activity with N-Succinyl-L-Pro
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.2
D-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
13.7
L-alanine
pH 10.0, 35°C, recombinant His-tagged enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-serine
0.12
0.15
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-asparagine
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
0.62
-
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
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
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
182
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°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
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
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
63
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
708.4
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
6.5 - 7.5
8.5
6.5 - 7.5
at a temperature of 60°C, the highest activity is detected at around pH 6.5-7.5
6.5 - 7.5
at 60°C, the highest activity is detected at around pH 6.5-7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
over 80% of maximal activity within this range, about 40% at pH 4.0, and about 50% at pH 11.0
7 - 10
activity range, over 50% of maximal activity at pH 8.0-9.5, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
95
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
activity range, RacX shows less than half of the activity at 37°C, almost inactive at 50°C, profile overview
25 - 50
activity range, activity increases from 25°C to 37°C and is highest at 37°C. Activity decreases from 40°C to 50°C, and is almost absent at 55°C, profile overview
50 - 80
the relative activities at 50°C and 80°C are 12% and 70%, respectively, as compared with that at 95°C
50 - 95
activity range, the relative activities at 50°C and 80°C are 12% and 70%, respectively, as compared with that at 95°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
brenda
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
brenda
bifunctional enzymes, racemization of serine and alpha,beta-elimination of L-serine
-
-
brenda
isoforms A and B, bifunctional enzymes, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
brenda
-
-
-
brenda
PH0138 gene encodes an amino acid racemase, AAR
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
DAR1 is localized to the medial region of the cerebral ganglion where the F- and C-clusters are situated
brenda
additional information
additional information
strain LK-145 is isolated from a Japanese sake seller as a high D-amino acid producer, and strain LT-13 is isolated from Moto, a starter of sake, as a low D-amino acid producer, using a medium of amylase digested rice as a carbon source
brenda
additional information
Latilactobacillus sakei LT-13
-
strain LK-145 is isolated from a Japanese sake seller as a high D-amino acid producer, and strain LT-13 is isolated from Moto, a starter of sake, as a low D-amino acid producer, using a medium of amylase digested rice as a carbon source
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the fold-type I PLP-dependent enzyme family
malfunction
the mutation of either Asp210 or Lys267 to alanine abolish the racemization activity for 2-aminohexano-6-lactam
metabolism
physiological function
additional information
metabolism
the enzyme is likely responsible for utilization of D-amino acids for growth
metabolism
-
the enzyme is likely responsible for utilization of D-amino acids for growth
-
physiological function
enzyme AAR is responsible for D-amino acid utilization in Pyrococcus horikoshii
physiological function
-
enzyme AAR is responsible for D-amino acid utilization in Pyrococcus horikoshii
-
additional information
analysis of the structure-function relationship, overview. Lys241 is a key amino acid residue, active site structure of ACL racemase. The substrate binding site is typically located between Trp49 and Tyr137. Lys241 Nepsilon is considered to be important for recognizing the carbonyl O of the substrate. Lys241 also forms a salt bridge with Glu396. Asp210 and Lys267 are two plausible acid/base catalytic candidate residues, situated on the re and si faces of the pyridoxal 5'-phosphate ring, respectively. The racemization of ACL racemase proceeds via a two-base mechanism
additional information
-
analysis of the structure-function relationship, overview. Lys241 is a key amino acid residue, active site structure of ACL racemase. The substrate binding site is typically located between Trp49 and Tyr137. Lys241 Nepsilon is considered to be important for recognizing the carbonyl O of the substrate. Lys241 also forms a salt bridge with Glu396. Asp210 and Lys267 are two plausible acid/base catalytic candidate residues, situated on the re and si faces of the pyridoxal 5'-phosphate ring, respectively. The racemization of ACL racemase proceeds via a two-base mechanism
additional information
conformational structure modeling of RacX based on the structure of Asp racemase from Pyrococcus horikoshi, PDB ID 1JFL
additional information
structural modeling of Ls-MalY, structure comparisons, overview
additional information
-
conformational structure modeling of RacX based on the structure of Asp racemase from Pyrococcus horikoshi, PDB ID 1JFL
-
additional information
Latilactobacillus sakei LT-13
-
structural modeling of Ls-MalY, structure comparisons, overview
-
Show AA Sequence and Transmembrane Helices (839 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
45000
91000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homohexamer
tetramer
-
gel filtration and analytical ultracentrifugation. Tetrameric structure in the absence or presence of Co2+, 4 * 42300 Da
additional information
homodimer
2 * 55800, recombinant enzyme, SDS-PAGE, 2 * 52100, about, sequence calculation
homodimer
-
2 * 55800, recombinant enzyme, SDS-PAGE, 2 * 52100, about, sequence calculation
-
homohexamer
6 * 46000, recombinant His6-tagged enzyme, SDS-PAGE
additional information
quaternary structure analysis of the enzyme using BN-PAGE, overview
additional information
-
quaternary structure analysis of the enzyme using BN-PAGE, overview
-
additional information
quaternary structure analysis of the enzyme using BN-PAGE, overview
additional information
Escherichia coli K-12 / MG1655
-
quaternary structure analysis of the enzyme using BN-PAGE, overview
-
additional information
structural modeling of Ls-MalY, structure comparisons, overview
additional information
Latilactobacillus sakei LT-13
-
structural modeling of Ls-MalY, structure comparisons, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
N-terminal signal sequence is cleaved off
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H152S
-
ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type
N154F
-
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
P153S
-
ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
Q155D
-
ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
I384M
I83L/D361V/Y396C
-
specific activity: 0.0303 (substrate Trp), 0.0257 (substrate Phe), 0.473 (substrate Lys), 0.0121 (substrate Ala)
L126H/Y396C
-
specific activity: 0.0524 (substrate Trp), 0.0436 (substrate Phe), 0.477 (substrate Lys), 0.0144 (substrate Ala)
R174A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R174K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. Mutant Bsar-R174K shows no deleterious effects on the transgenic plants and broad range amino acid racemase activity, might serve as a good selection marker
Y293A/Y301S/Y396C
-
specific activity: 0.0267 (substrate Trp), 0.0249 (substrate Phe), 0.458 (substrate Lys), 0.0141 (substrate Ala)
Y396C
-
specific activity: 0.0487 (substrate Trp), 0.00706 (substrate Phe), 0.03215 (substrate Lys), 0.825 (substrate Ala)
R174A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
R174K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. Mutant Bsar-R174K shows no deleterious effects on the transgenic plants and broad range amino acid racemase activity, might serve as a good selection marker
-
additional information
I384M
-
I384M mutant BAR shows the highest activity for Trp. Using I384M mutant BAR the proportion of D-Trp reaches 43% while wildtype BAR racemizes only 6% of initial L-Trp
I384M
-
specific activity: 0.124 (substrate Trp), 0.0744 (substrate Phe), 0.223 (substrate Lys), 0.026 (substrate Ala)
additional information
-
for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. Enzyme AAR is not a suitable candidate compared to enzyme Lyr (EC 5.1.1.5) from Proteus mirabilis
additional information
-
for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. Enzyme AAR is not a suitable candidate compared to enzyme Lyr (EC 5.1.1.5) from Proteus mirabilis
-
additional information
-
random mutagenesis on bar gene is performed to obtain mutant BAR derivates with high activity for Trp. Five positive mutant are isolated after the two-step-screening of the randomly mutated BAR
additional information
-
substitutions at Y396 and I384 increases the Trp specific racemization activity and the racemazation activity for overall amino acids, respectively
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
the enzyme shows little racemase activity below pH 6.5 and an increasing activity between pH 7.0-8.5 in 50 mM Tris-HCl buffer
715591
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14 - 50
-
the enzyme activity increases between 14-45°C and starts to decrease at 50°C for both the Ser and Asp conversion
60
80
60
-
GkNSAAR shows a gradual loss of activity at preincubation temperatures over 60°C
80
enzyme retains its full activity after incubation at 80°C for at least 2 h in buffer pH 7-10
80
purified enzyme protein at 80°C for 2 h under various pH conditions, BAR shows no loss of activity at pHs ranging from pH 7.0 to pH 10.0. At pH 7.0, the enzyme retains its full activity, even after incubation at 80°C for 24 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
buffer without organic content provides excellent stability at moderate temperatures (20–35°C) while addition of 20% acetonitrile or methanol drastically reduces the half-life of the racemase
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-5°C, 0.01 M potassium phosphate buffer, pH 7.0, 2 mM pyridoxal 5'-phosphate, 1 month, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli with N-terminal His-tag, purification protocol from inclusion bodies
-
protein is purified by applying to a diethylaminoethyl sepharose fast flow column and a phenyl sepharose 6 fast flow column
-
purified in a one-step procedure by immobilized cobalt affinity chromatography
-
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, to homogeneity
recombinant soluble enzyme BAR from Escherichia coli strain BL21(DE3) by heat treatment at 90°C for 20 min, ammonium sulfate fractionation, and hydrophobic interaction chromatography, dialysis, anion echange chromatography, and again dialysis
two enzyme lyophilisates of different purity are obtained from which the crude is sufficient for the racemization of methionine and the pure is used for asparagine
-
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amino acid racemase of Pseudomonas putida DSM 3263 is overexpressed in Escherichia coli and delivered cell free extract with easily sufficient activity (20–50 U/mg total protein) for application in an enzyme membrane reactor (EMR) setting
-
enzyme is produced mainly as an inclusion body in Escherichia coli. In this study, expression of the recombinant protein into the soluble fraction is markedly improved by coexpression with chaperone molecules
gene AAR, recombinant expression in Escherichia coli strain BL21(DE3), showing lower lysine racemase activity, protein AAR is highly insoluble 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, 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 malY, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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 racX, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
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 ygeA, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
over-expressed in Escherichia coli
recombinant expression of enzyme BAR in inclusion bodies in Escherichia coli strain BL21(DE3), expression of the recombinant protein in the soluble fraction is markedly improved by co-expression with chaperone molecules, i.e. chaperone proteins DnaK-DnaJ-GrpE and GroEL-GroES, GroELGroES and Tig, and Tig, method optimization
recombinant overexpression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) and complementation of lysine or asparagine auxotroph strains (Escherichia coli lysine auxotrophic strain BCRC 51734 and asparagine auxotrophic strain CGSC 4813) recombinant expression of wild-type and mutant enzymes in Arabidopsis thaliana ecotype Columbia and Oryza sativa cv. Tainung 67 plants using the Agrobacterium tumefaciens strain EHA105 transformation system. The Bsar variant, Bsar-R174K, is useful as a selectable marker gene in Arabidopsis and rice that are susceptible to L-lysine and D-alanine. The transformation of Arabidopsis thalinana with Bsar or Bsar variants based on D-alanine selection reveals that Bsar-R174K has the greatest efficiency (2.40%), superior to kanamycin selection-based transformation (1.10%). L-lysine-based selection exhibits lower efficiency for Bsar-R174K (0.17%). The progenies of selected Bsar-R174K transgenic Arabidopsis thaliana plants reveals normal growth properties. Bsar-R174K mutant transgenic Oryza sativa is obtained on L-lysine medium with an efficiency of 0.9%, and the progenies of the transgenic rice show morphologically normal phenotypes comparable with their wild-type counterparts. RT-PCR expression analysis
-
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity is enhanced in cells grown in the medium supplemented with D-amino acids especially D-allo-Ile
activity is enhanced in cells grown in the medium supplemented with D-amino acids especially D-allo-Ile
activity is enhanced in cells grown in the medium supplemented with D-amino acids especially D-allo-Ile
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
simple procedure for in situ analysis of stereospecificity of C-4 hydrogen transfer of NADH by an NAD-dependent dehydrogenase by combination with amino acid racemase, EC 5.1.1.10, and L-leucine dehydrogenase, EC 1.4.1.9
biotechnology
diagnostics
synthesis
biotechnology
-
since commercially available D-Trp is chemically synthesized and expensive a mutant BAR protein might represent an effective method to synthesize D-Trp
biotechnology
-
an enzyme lyophilisate of amino acid racemase from Pseudomonas putida is used for in situ racemization. Crystallization experiments accompanied by enzymatic racemization lead to a significant increase of crystallized L-Asn
diagnostics
-
broad-specificity amino acid racemase is a non-antibiotic selectable marker for transgenic plants and can be used in the development of genetically modified plants without using antibiotic resistance marker genes. Selection with different amino acid enantiomers using Bsar, Bsar-R174A and Bsar-R174K gene as selectable markers, overview
diagnostics
-
broad-specificity amino acid racemase is a non-antibiotic selectable marker for transgenic plants and can be used in the development of genetically modified plants without using antibiotic resistance marker genes. Selection with different amino acid enantiomers using Bsar, Bsar-R174A and Bsar-R174K gene as selectable markers, overview
-
synthesis
-
enzymatic production of L-Trp from DL-Ser and indole by a coupled reaction of tryptophan synthase and amino acid racemase
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the high reactivity toward Trp and Tyr, as well as extremely high thermostability, is likely a major advantage of using BAR for biochemical conversion of these aromatic amino acids
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
Glutamicibacter nicotianae NCIMB 41126
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
Brucella anthropi IA / NCBIMB41129
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the high reactivity toward Trp and Tyr, as well as extremely high thermostability, is likely a major advantage of using BAR for biochemical conversion of these aromatic amino acids
-
synthesis
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
Enzymatic production of L-tryptophan from DL-serine and indole by a coupled reaction of tryptophan synthase and amino acid racemase
Biotechnol. Appl. Biochem.
12
141-149
1990
Pseudomonas putida
brenda
Reynolds, K.; Martin, J.; Shen, S.J.; Esaki, N.; Soda, K.; Floss, H.G.
Mechanistic studies of two amino acid racemases of broad substrate specificity from Pseudomonas striata and Aeromonas caviae
J. Basic Microbiol.
31
177-188
1991
Aeromonas caviae, Pseudomonas putida
brenda
Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.
Purification and properties of amino acid racemase from Aeromonas punctata subsp. caviae
Prog. Clin. Biol. Res.
144A
355-363
1984
Aeromonas caviae
brenda
Esaki, N.; Shimoi, H.; Nakajima, N.; Oshima, T.; Tanaka, H.; Soda, K.
Enzymatic in situ determination of stereospecificity of NAD-dependent dehydrogenases
J. Biol. Chem.
264
9750-9752
1989
Bacteria
brenda
Adams, E.
Amino acid racemases and epimerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
479-507
1972
Pseudomonas putida
-
brenda
Strisovsky, K.; Jiraskova, J.; Mikulova, A.; Rulisek, L.; Konvalinka, J.
Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity
Biochemistry
44
13091-13100
2005
Mus musculus
brenda
Strisovsky, K.; Jiraskova, J.; Barinka, C.; Majer, P.; Rojas, C.; Slusher, B.S.; Konvalinka, J.
Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate
FEBS Lett.
535
44-48
2003
Mus musculus
brenda
Foltyn, V.N.; Bendikov, I.; De Miranda, J.; Panizzutti, R.; Dumin, E.; Shleper, M.; Li, P.; Toney, M.D.; Kartvelishvily, E.; Wolosker, H.
Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity
J. Biol. Chem.
280
1754-1763
2005
Mus musculus
brenda
Neidle, A.; Dunlop, D.S.
Allosteric regulation of mouse brain serine racemase
Neurochem. Res.
27
1719-1724
2002
Mus musculus
brenda
Nagayoshi, C.; Ishibashi, M.; Kita, Y.; Matsuoka, M.; Nishimoto, I.; Tokunaga, M.
Expression, refolding and characterization of human brain serine racemase in Escherichia coli with N-terminal His-tag
Protein Pept. Lett.
12
487-490
2005
Homo sapiens
brenda
Kino, K.; Sato, M.; Yoneyama, M.; Kirimura, K.
Synthesis of DL-tryptophan by modified broad specificity amino acid racemase from Pseudomonas putida IFO 12996
Appl. Microbiol. Biotechnol.
73
1299-1305
2007
Pseudomonas putida
brenda
Sakai, A.; Xiang, D.F.; Xu, C.; Song, L.; Yew, W.S.; Raushel, F.M.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway for the irreversible conversion of D- to L-amino acids
Biochemistry
45
4455-4462
2006
Geobacillus kaustophilus
brenda
Bechtold, M.; Makart, S.; Reiss, R.; Alder, P.; Panke, S.
Model-based characterization of an amino acid racemase from Pseudomonas putida DSM 3263 for application in medium-constrained continuous processes
Biotechnol. Bioeng.
98
812-824
2007
Pseudomonas putida
brenda
Matsui, D.; Oikawa, T.; Arakawa, N.; Osumi, S.; Lausberg, F.; Staebler, N.; Freudl, R.; Eggeling, L.
A periplasmic, pyridoxal-5-phosphate-dependent amino acid racemase in Pseudomonas taetrolens
Appl. Microbiol. Biotechnol.
83
1045-1054
2009
Pseudomonas taetrolens (I0J1I6), Pseudomonas taetrolens
brenda
Pozo-Dengra, J.; Martinez-Rodriguez, S.; Contreras, L.M.; Prieto, J.; Andujar-Sanchez, M.; Clemente-Jimenez, J.M.; Las Heras-Vazquez, F.J.; Rodriguez-Vico, F.; Neira, J.L.
Structure and conformational stability of a tetrameric thermostable N-succinylamino acid racemase
Biopolymers
91
757-772
2009
Geobacillus kaustophilus
brenda
Wuerges, K.; Petrusevska-Seebach, K.; Elsner, M.P.; Luetz, S.
Enzyme-assisted physicochemical enantioseparation processes-Part III: Overcoming yield limitations by dynamic kinetic resolution of asparagine via preferential crystallization and enzymatic racemization
Biotechnol. Bioeng.
104
1235-1239
2009
Pseudomonas putida
brenda
Würges, K.; Petrusevska, K.; Serci, S.; Wilhelm, S.; Wandrey, C.; Seidel-Morgenstern, A.; Elsner, M.; Lütz, S.
Enzyme-assisted physicochemical enantioseparation processes: Part I. Production and characterization of a recombinant amino acid racemase
J. Mol. Catal. B
58
10-16
2009
Pseudomonas putida
-
brenda
Pozo-Dengra, J.; Martínez-Gómez, A.; Martínez-Rodríguez, S.; Clemente-Jiménez, J.; Rodríguez-Vico, F.; Heras-Vázquez, F.
Racemization study on different N-acetylamino acids by a recombinant N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264
Process Biochem.
44
835-841
2009
Geobacillus kaustophilus
-
brenda
Wang, L.; Ota, N.; Romanova, E.V.; Sweedler, J.V.
A novel pyridoxal 5'-phosphate-dependent amino acid racemase in the Aplysia californica central nervous system
J. Biol. Chem.
286
13765-13774
2011
Aplysia californica
brenda
Kawakami, R.; Ohmori, T.; Sakuraba, H.; Ohshima, T.
Identification of a novel amino acid racemase from a hyperthermophilic archaeon Pyrococcus horikoshii OT-3 induced by D-amino acids
Amino Acids
47
1579-1587
2015
Pyrococcus horikoshii (O57878), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O57878)
brenda
Kawakami, R.; Sakuraba, H.; Ohmori, T.; Ohshima, T.
First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3
J. Biosci. Bioeng.
124
23-27
2017
Pyrococcus horikoshii (O57878), Pyrococcus horikoshii OT-3 (O57878)
brenda
Miyamoto, T.; Katane, M.; Saitoh, Y.; Sekine, M.; Homma, H.
Identification and characterization of novel broad-spectrum amino acid racemases from Escherichia coli and Bacillus subtilis
Amino Acids
49
1885-1894
2017
Escherichia coli (P03813), Bacillus subtilis (P32960), Bacillus subtilis 168 (P32960), Escherichia coli K-12 / MG1655 (P03813)
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, Citreicella sp. SE45, Mycolicibacterium vanbaalenii (A1T974), Janibacter sp. HTCC2649 (A3TM80), Sinorhizobium medicae (A6UKD1), Brucella anthropi (A6X7I5), Brucella anthropi (Q06K28), Brucella anthropi, Mesorhizobium opportunistum (F7Y223), Sinorhizobium meliloti (H0FT96), Sinorhizobium meliloti (Q92MM4), Achromobacter obae (Q7M181), Achromobacter obae, 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 (Q06K28), Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 (A6X7I5)
brenda
Wang, X.; Yang, L.; Cao, W.; Ying, H.; Chen, K.; Ouyang, P.
Efficient production of enantiopure D-lysine from L-lysine by a two-enzyme cascade system
Catalysts
6
168-178
2016
Lacticaseibacillus paracasei, Lacticaseibacillus paracasei ATCC 334
-
brenda
Kato, S.; Oikawa, T.
A novel bifunctional amino acid racemase with multiple substrate specificity, malY from Lactobacillus sakei LT-13 Genome-based identification and enzymological characterization
Front. Microbiol.
9
403
2018
Latilactobacillus sakei (A0A223K4L6), Latilactobacillus sakei LT-13 (A0A223K4L6)
brenda
Kuan, Y.; Thiruvengadam, V.; Lin, J.; Liu, J.; Chen, T.; Wu, H.; Wang, W.; Chen, L.
Broad-specificity amino acid racemase, a novel non-antibiotic selectable marker for transgenic plants
Plant Biotechnol. Rep.
12
27-38
2018
Pseudomonas putida, Pseudomonas putida DSM 84
-
brenda
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