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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
- 5'-phosphate
- synthesis
-
plp-dependent
-
5'-phosphate-dependent
- buchneri
-
2-epimerase
-
alpha-hydrogen
- biotechnology
- analysis
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AAR, ACL racemase, amino acid racemase, amino-acid racemase, ArgR, BAR, broad specificity amino acid racemase, broad substrate specificity amino acid racemase, broad-specificity amino acid racemase, broad-spectrum amino 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
Ochrobactrum 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
-
-
-
-
an L-amino acid = a D-amino acid
significant internal return of the alpha-hydrogen; single base mechanism
-
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
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
the racemization of ACL racemase proceeds via a two-base mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
D-ornithine
D-ornithine
46.7% activity compared to LL-diaLinopimelate
-
-
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
-
-
L-serine
S-serine
-
similar substrate affinity for both L-serine and D-serine
-
-
?
L-threonine
3-hydroxy-2-butenoic acid + NH3
-
alpha,beta-elimination reaction
-
-
?
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
Ochrobactrum 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-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-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-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
Ochrobactrum anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
-
-
r
L-alanine amide
D-alanine amide
Ochrobactrum 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-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
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-Methionine
D-Methionine
Escherichia coli K-12 / MG1655
7.9% 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
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
?
-
-
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
?
-
D0D2T1
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
?
-
D0D2T1
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
?
-
Janibacter sp. HTCC 2649
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
?
-
Janibacter sp. HTCC 2649
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
?
-
Lactobacillus 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
?
-
Lactobacillus 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
?
-
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
?
-
Ochrobactrum 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
?
-
Ochrobactrum 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
?
-
Ochrobactrum 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
?
-
Ochrobactrum 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
?
-
-
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
?
-
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
?
-
D0D2T1
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
?
-
Janibacter sp. HTCC 2649
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
?
-
Lactobacillus 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 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
?
-
Ochrobactrum 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
?
-
Ochrobactrum 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 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; Km: 0.2 mM
pyridoxal 5'-phosphate
-
holoenzyme contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme; Km: 0.0026 mM; required for maximal activity
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of subunit; 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; Km: 0.0026 mM
pyridoxal 5'-phosphate
-
holoenzyme contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme; pyridoxal phosphate enzyme
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; dependent on
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
30
L-Met
-
crude lyophilisates, 25°C, pH 6, Vmax: 1174 micromol/min/g; crude lyophilisates, 30°C, pH 7, Vmax: 2296 micromol/min/g
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
-
no activity with N-Succinyl-L-Pro
-
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
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
additional information
additional information
-
no activity with N-Succinyl-L-Pro; N-Succinyl-L-Cys, low specific rotation prevented kinetic analysis; 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.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.12
-
purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-alanine; purified recombinant mutant R174K, pH 7.0, 37°C, substrate L-methionine
0.15
-
purified recombinant mutant R174A, pH 7.0, 37°C, substrate L-asparagine
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
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
D0D2T1
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
D0D2T1
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%
63
purified enzyme, substrate D-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
at 60°C, the highest activity is detected at around pH 6.5-7.5; at a temperature of 60°C, the highest activity is detected at around pH 6.5-7.5
8.5
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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
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE