Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution

alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
evolution
-
the enzyme shows evolutionary and structural similarity to the promiscuous enzymes serine hydroxymethyltransferase, EC 2.1.2.1, and threonine aldolase, EC 4.1.2.48. The three enzymes represent a model of divergent evolution from an ancestral enzyme that was able to catalyse all the reactions of the modern enzymes. Similarly to serine hydroxymethyltransferase and threonine aldolase, Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions
evolution
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
evolution
-
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
-
malfunction

during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 10fold, and no viable bacteria are present at 24 h
malfunction
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages; during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages
malfunction
because D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of alanine racemase is lethal to prokaryotes
malfunction
-
depletion of D-alanine results in rapid loss of viability. The alr mutant is defective for growth in macrophages
malfunction
-
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 10fold, and no viable bacteria are present at 24 h
-
malfunction
-
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages; during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages
-
malfunction
-
depletion of D-alanine results in rapid loss of viability. The alr mutant is defective for growth in macrophages
-
malfunction
-
because D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of alanine racemase is lethal to prokaryotes
-
metabolism

-
important for cell wall biosynthesis
metabolism
-
biosynthesis of D-alanine as building blocks in the peptidoglycan layers of bacterial cell walls
metabolism
important for peptidoglycan biosynthesis
metabolism
-
important for peptidoglycan biosynthesis
metabolism
-
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
-
important for peptidoglycan biosynthesis
metabolism
-
important for peptidoglycan biosynthesis
metabolism
-
plays a role in spore germination and cell wall biosynthesis
metabolism
-
important for peptidoglycan biosynthesis
-
physiological function

-
alanine racemase plays an essential role in cell wall synthesis as it racemizes L-alanine into D-alanine, a key building block in the biosynthesis of peptidoglycan
physiological function
-
alanine racemase catalyzes the racemization of L-alanine to D-alanine, which is a key component of the peptidoglycan layer, especially in cross-linking the bacterial cell walls
physiological function
-
the pyridoxal 5'-phosphate-dependent enzyme alanine racemase produces the D-alanine incorporated in the cyclic peptide cyclosporine A synthesized by the fungus
physiological function
-
involvement of alanine racemase in germination of Bacillus cereus spores lacking an intact exosporium. L-Alanine-mediated germination of food isolated Bacillus cereus DSA 1 spores, which lack an intact exosporium, is increased in the presence of D-cycloserine, an alanine racemase inhibitor, reflecting the activity of the Alr enzyme, capable of converting L-alanine to the germination inhibitor D-alanine, contribution of alanine racemase to the autoinhibition of Bacillus cereus spore germination
physiological function
-
the enzyme is essential for the organism, it is not possible to generate an alr knockout mutant in the absence of a complementing gene copy or D-alanine in the growth medium
physiological function
-
alanine racemase catalyzes the racemization of L-alanine to D-alanine, which is a key component of the peptidoglycan layer, especially in cross-linking the bacterial cell walls
-
physiological function
-
involvement of alanine racemase in germination of Bacillus cereus spores lacking an intact exosporium. L-Alanine-mediated germination of food isolated Bacillus cereus DSA 1 spores, which lack an intact exosporium, is increased in the presence of D-cycloserine, an alanine racemase inhibitor, reflecting the activity of the Alr enzyme, capable of converting L-alanine to the germination inhibitor D-alanine, contribution of alanine racemase to the autoinhibition of Bacillus cereus spore germination
-
physiological function
-
the enzyme is essential for the organism, it is not possible to generate an alr knockout mutant in the absence of a complementing gene copy or D-alanine in the growth medium
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-lysine
L-lysine
-
enzyme mutant I222T/Y354W, no activity with the wild-type enzyme
-
-
?
D-serine
L-serine
-
-
-
-
r
L-2-Aminobutyrate
D-2-Aminobutyrate
0.37% of the activity with L-Ala
-
r
L-2-aminobutyric acid
D-2-aminobutyric acid
-
18% of the activity with L-Ala
-
?
L-alanine
R-alanine
-
-
-
r
L-Arg
D-Arg
-
stepwise mechanism for alanine racemase at both 25°C and at 65°C. The carbanionic intermediate is obligatory, and Arg219 may serve to destabilize it to avoid side reactions such as transamination, a detailed reaction mechanism is proposed that includes enzyme and substrate protonation states
-
r
L-arginine
D-arginine
less than 10% activity compared to L-alanine
-
-
r
L-isoleucine
D-isoleucine
L-Methionine
D-Methionine
less than 10% activity compared to L-alanine
-
-
r
L-phenylalanine
D-phenylalanine
1.1% activity compared to L-alanine
-
-
r
L-proline
D-proline
1.1% activity compared to L-alanine
-
-
r
L-valine
D-valine
less than 10% activity compared to L-alanine
-
-
r
additional information
?
-
D-alanine

L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
?
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
L-Ala

?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala

D-Ala
-
highly specific for Ala
-
r
L-Ala
D-Ala
-
highly specific for Ala
-
r
L-Ala
D-Ala
-
specific for Ala
-
-
L-Ala
D-Ala
-
specific for Ala
-
-
L-Ala
D-Ala
-
the enzyme catalyzes transamination as a side function.The pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH
-
r
L-Ala
D-Ala
-
Tyr265 and Lys39 are the catalytic bases removing alpha-hydrogen from L- and D-alanine
-
r
L-Ala
D-Ala
-
the enzyme catalyzes the first committed step in bacterial cell wall biosynthesis
-
?
L-Ala
D-Ala
-
highly specific for Ala
-
r
L-Ala
D-Ala
-
the ratio of the activity for conversion of D-alanine to L-alanine to that of the reverse conversion is constantly about 0.5 in the pH range 7-9.5
-
r
L-Ala
D-Ala
-
enzyme is required for production of D-Ala, a necessary component of the bacterial cell wall
-
?
L-alanine

D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
alanine racemase can discriminate effectively between L-alanine and L-2-aminobutyric acid, and selectively and reversibly catalyzes L-alanine to D-alanine transformation Therefore, the enzyme shows ability of eliminating L-Ala from the reaction mixtures of L-2-aminobutyric acid biosynthesis, method optimization and evaluation in a coupled reaction with D-amino acid oxidase converting D-alanine to pyruvate stereoselectively, overview
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
Q208U6
-
-
-
r
L-alanine
D-alanine
-
-
?
L-alanine
D-alanine
-
-
responsible for the synthesis of the d-alanine moiety present in cyclosporin A and of HC-toxin
-
-
L-alanine
D-alanine
TOXG encodes an alanine racemase whose function is to synthesize D-Ala for incorporation into HC-toxin, enzyme is involved in cyclic peptide biosynthesis
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine, highly preferred substrate
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
first step in the biosynthesis of the peptidoglycan
-
-
?
L-alanine
D-alanine
-
The bacterium utilizes D-alanine (DAla) for synthesis of the peptidoglycan cell wall.
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
a major component of the alanine pathway, D-alanine is a major component in cell wall synthesis
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
optimal substrate for alanine racemase
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
optimal substrate for alanine racemase
-
-
?
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
responsible for the synthesis of the d-alanine moiety present in cyclosporin A and of HC-toxin
-
-
-
L-alanine
D-alanine
-
reversible reaction from an external aldimine in both directions via a quinonoid intermediate, overview
-
-
r
L-isoleucine

D-isoleucine
-
-
-
-
?
L-isoleucine
D-isoleucine
-
-
-
-
?
L-leucine

D-leucine
-
activity is 20% compared with L-alanine, other amino acids are not racemized
-
-
r
L-leucine
D-leucine
0.9% activity compared to L-alanine
-
-
r
L-lysine

D-lysine
less than 10% activity compared to L-alanine
-
-
r
L-lysine
D-lysine
-
enzyme mutant I222T/Y354W, no activity with the wild-type enzyme
-
-
?
L-Ser

D-Ser
-
50% of the activity with L-Ala
-
?
L-Ser
D-Ser
-
at 0.5% of the activity with L-Ala
-
?
L-Ser
D-Ser
-
40% of the activity with L-Ala
-
-
?
L-Ser
D-Ser
3.7% of the activity with L-Ala
-
r
L-Ser
D-Ser
2% of the activity with L-Ala
-
r
L-serine

D-serine
less than 10% activity compared to L-alanine
-
-
r
L-serine
D-serine
-
-
-
-
r
additional information

?
-
-
exchange of the alpha-hydrogen of D-Ala and L-Ala with D2O
-
-
-
additional information
?
-
high specificity to L-alanine, low activity with L-arginine, L-methionine, L-lysine, L-serine, L-valine, L-proline, L-phenylalanine, L-leucine, respectively, no activity with L-histidine
-
-
-
additional information
?
-
-
the enzyme catalyzes transamination as side reaction, R-isomer preference in the hydrogen abstraction from pyridoxamine 5'-phosphate
-
?
additional information
?
-
-
the epsilon-amino group of Lys39 participates in both racemization and transamination when catalyzed by the wild-type enzyme
-
?
additional information
?
-
-
residues Ile222 and Tyr354 are important for the enzyme substrate specificity
-
-
-
additional information
?
-
-
no racemization of L-Ser, L-Asp, L-Glu, L-Val and L-Arg
-
?
additional information
?
-
-
the enzyme is only specific to L-alanine and L-isoleucine, and does not catalyze isomerization the other amino acids
-
-
-
additional information
?
-
-
the enzyme is only specific to L-alanine and L-isoleucine, and does not catalyze isomerization the other amino acids
-
-
-
additional information
?
-
-
alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala
-
-
-
additional information
?
-
-
alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala
-
-
-
additional information
?
-
-
two nonhomologous alanine racemase genes, one of which is associated with the catabolic function and the other of which presumably represents the biosynthetic function
-
-
-
additional information
?
-
-
specific for alanine
-
-
-
additional information
?
-
-
key enzyme in cyclosporin A biosynthesis
-
-
-
additional information
?
-
-
Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions, kinetic analysis and reaction mechanisms, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-alanine
R-alanine
P0A6B4
-
-
-
r
additional information
?
-
D-alanine

L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
P0A2W8
-
-
-
r
L-Ala

?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
-
L-Ala

D-Ala
-
the enzyme catalyzes the first committed step in bacterial cell wall biosynthesis
-
?
L-Ala
D-Ala
-
enzyme is required for production of D-Ala, a necessary component of the bacterial cell wall
-
?
L-alanine

D-alanine
A1XDT8
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
Q81VF6
-
enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
P10725, P94494
-
-
-
r
L-alanine
D-alanine
P10725, P94494
-
-
-
r
L-alanine
D-alanine
Q208U6
-
-
-
r
L-alanine
D-alanine
-
-
responsible for the synthesis of the d-alanine moiety present in cyclosporin A and of HC-toxin
-
-
L-alanine
D-alanine
Q9UW18
TOXG encodes an alanine racemase whose function is to synthesize D-Ala for incorporation into HC-toxin, enzyme is involved in cyclic peptide biosynthesis
-
?
L-alanine
D-alanine
Q8RAK6
-
-
-
r
L-alanine
D-alanine
Q8R860
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
Q837J0
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
first step in the biosynthesis of the peptidoglycan
-
-
?
L-alanine
D-alanine
-
The bacterium utilizes D-alanine (DAla) for synthesis of the peptidoglycan cell wall.
-
-
r
L-alanine
D-alanine
P45257
-
-
-
r
L-alanine
D-alanine
Q1XG01
-
-
-
r
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
B9WYE8
-
-
-
r
L-alanine
D-alanine
-
a major component of the alanine pathway, D-alanine is a major component in cell wall synthesis
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
Q04DI1
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
Q04DI1
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
-
L-alanine
D-alanine
P63479
-
-
-
r
L-alanine
D-alanine
P63479
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
responsible for the synthesis of the d-alanine moiety present in cyclosporin A and of HC-toxin
-
-
-
additional information

?
-
-
alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala
-
-
-
additional information
?
-
-
alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala
-
-
-
additional information
?
-
-
two nonhomologous alanine racemase genes, one of which is associated with the catabolic function and the other of which presumably represents the biosynthetic function
-
-
-
additional information
?
-
-
key enzyme in cyclosporin A biosynthesis
-
-
-
additional information
?
-
-
Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions, kinetic analysis and reaction mechanisms, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FAD
-
not required as cofactor, slight activation at low concentrations, inhibition at high concentrations
pyridoxal 5'-phosphate

-
required as coenzyme
pyridoxal 5'-phosphate
-
1 mol of pyridoxal 5'-phosphate is bound per subunit
pyridoxal 5'-phosphate
-
1 pyridoxal 5'-phosphate per 42000 MW subunit
pyridoxal 5'-phosphate
-
contains one mol of pyridoxal 5'-phosphate per mol of enzyme; Km: 0.000033 mM; the sequence of 10 amino acid residues around the Lys residue, to which pyridoxal 5'-phosphate is bound, is identical with that of the dadB racemase
pyridoxal 5'-phosphate
-
2 mol of pyridoxal 5'-phosphate bound per mol of enzyme dimer
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
the monomeric inactive enzyme appears to bind the cofactor pyridoxal 5'-phosphate by a non-covalent linkage, although the native dimeric enzyme binds the cofactor through an aldimine Schiff base linkage
pyridoxal 5'-phosphate
-
2 mol of pyridoxal 5'-phosphate bound per mol of enzyme dimer
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated; pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated; pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated; pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated; pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
not required as cofactor, slight activation at low concentrations, inhibition at high concentrations
pyridoxal 5'-phosphate
-
required as coenzyme
pyridoxal 5'-phosphate
-
Arg219 forms a hydrogen bond with the pyridine nitrogen of the cofactor, Arg136 donates a hydrogen bond to the phenolic oxygen of pyridoxal 5'-phosphate and may be involved in the binding of substrate as well as stabilization of intermediates
pyridoxal 5'-phosphate
Km: 0.005 mM, at 30°C
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
-
both active sites of the dimer contain a pyridoxal 5'-phosphate molecule in aldimine linkage to Lys39 as a protonated Schiff base. The protonated pyridoxal 5'-phosphate-Lys39 Schiff base is the reactive form of the enzyme
pyridoxal 5'-phosphate
-
each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the pyridoxal 5'-phosphate cofactor and a second domain primarily composed of beta-strands. The cofactor adopts two partially occupied conformational states that resemble previously reported and external aldimine complexes
pyridoxal 5'-phosphate
-
1 mol of enzyme contains 2 mol of cofactor
pyridoxal 5'-phosphate
-
enzyme is dependent on, maximal activity at 0.025 mM
pyridoxal 5'-phosphate
-
Km at 30°C is 0.005 mM. Maximal activity is obtained in presence of more than 0.125 mM pyridoxal 5'-phosphate. The decrease in activity at incubation temperatures over 40°C is consistent with the decrease in the amount of bound pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
coenzyme
pyridoxal 5'-phosphate
-
the pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH
pyridoxal 5'-phosphate
-
1 mol per mol of enzyme
pyridoxal 5'-phosphate
-
enzyme is dependent on
pyridoxal 5'-phosphate
-
covalently linked to enzyme at K42
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
C-terminal region of 1 subdomain: Arg138 donates a hydrogen bond to the phenolic O atom of PLP, Arg224 donates a hydrogen bond to the pyridinyl N atom of PLP, Lys41 forms an aldimine linkage with the PLP, eliminating water to form the Schiff base, C-terminal atoms of second subunit Ser209, Gly226 and Ile227 stabilize the PLP phosphate with the help of Ser209 O(gamma), Tyr45 O(eta) and Tyr359 O(eta)
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
pyridoxal 5'-phosphate
-
once per 1 million turnovers of racemization a H-atom is added to C4-atom of the substrate moiety of the anionic intermediate instead of the reprotonation of the abstracted hydrogen at C(alpha) resulting in pyridoxamine 5'-phosphate
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
PLP is inherently bound to the enzyme, removal of PLP inactivates the enzyme, adding PLP restores the activity, addition of 10 microM PLP to native enzyme slightly enhances activity
pyridoxal 5'-phosphate
PLP is bound to the enzyme, adding PLP during developement of enzyme or to an assay is not necessary
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on, pyridoxal 5'-phosphate is bound to each monomer of the dimeric enzyme and forms a Schiff base with Lys39
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on, alanine racemase requires pyridoxal-5'-phosphate as a cofactor to form a Schiff base between pyridoxal 5'-phosphate and epsilon-amino group of the lysine residue in the active site
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
additional information

-
contains a pyridoxal 5'-phosphate binding site
-
additional information
-
exogenous pyridoxal 5’-phosphate is not required, but enzyme may be pyridoxal 5’-phosphate-dependent
-
additional information
-
not activated by pyridoxal 5'-phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1-Aminoethyl)boronic acid
-
-
(1-Aminoethyl)phosphonate
(4R)-4-amino-3-isoxazolidinone
-
-
(R)-1-aminoethylphosphonic acid
1,1'-(2-oxido-1,2,5-oxadiazole-3,4-diyl)-bis (1-(2-thienyl))-methanone
-
-
1-amino-cyclopropane phosphonate
-
-
2-(2-hydroxyphenoxy)-N-methylacetamide
-
-
2-(4,6-dimethyl-3-oxo-[1,2]thiazolo[5,4-b]pyridin-2-yl)-N-[2-(4-ethoxyphenyl)ethyl]acetamide
-
-
2-(4-methoxyphenyl)-1-morpholin-4-ylethanethione
-
-
2-(4-methylphenyl)-1-morpholin-4-ylethanethione
-
-
2-(hydoxyimino)-6-methyl-2H-benzopyran-3-carboxamide
-
-
2-(pyridin-3-ylcarbamothioyl sulfanyl)acetic acid
-
-
2-Amino-3-chlorobut-3-enoic acid
2-Amino-3-fluorobut-3-enoic acid
2-N',2-N',7-N',7-N'-tetramethyl-9H-fluorene-2,7-disulfonohydrazide
-
-
2-phenyl-1-piperidin-1-ylethanethione
-
-
3,3-dihydroxy-1H-quinoline-2,4-dione
-
-
5-chloro-N-(3-chloro-4-methoxyphenyl)-2-(methylsulfonyl)pyrimidine-4-carboxamide
-
-
6-O-[3-chloro-4-(6-methoxycarbonylpyridine-2-carbonyl)oxyphenyl] 2-O-methyl pyridine-2,6-dicarboxylate
-
-
Aminooxyacetate
-
1 mM, complete inhibition, both directions
beta,beta,beta-trifluoroalanine
Cu2+
-
40% residual activity at 1 mM
D-penicillamine
-
1 mM, 79% inhibition
ethyl 3-(pyridin-2-ylthio)propanoate
-
-
FAD
-
slight activation at low concentrations, inhibition at high concentrations
L-alanine phosphonic acid
-
-
L-Penicillamine
-
1 mM, 28% inhibition
N',N',4-trimethylbenzenesulfonohydrazide
-
-
N-benzyl-5-chloro-2-methylsulfonylpyrimidine-4-carboxamide
-
-
N-hydroxy-2-(2-hydroxyphenoxy)acetamide
-
-
NaBH4
-
0.5 M, loss of activity
NEM
-
1 mM, 22% inhibition
O-Carbamoyl-D-Ser
-
inhibition of wild type enzyme but not of the O-carbamoyl-D-Ser mutant
PCMB
-
1 mM, 91% inhibition
(1-Aminoethyl)phosphonate

-
D- and L-(1-aminoethyl)phosphonate
(1-Aminoethyl)phosphonate
-
-
(R)-1-aminoethylphosphonic acid

-
in combination with pyridoxal 5'-phosphate
(R)-1-aminoethylphosphonic acid
-
upon formation of the external aldimine the phosphonate group interacts with putative catalytic residues, thereby rendering them unavailable for catalysis
2-Amino-3-chlorobut-3-enoic acid

-
i.e. 3-chlorovinylglycine, irreversible
2-Amino-3-chlorobut-3-enoic acid
-
-
2-Amino-3-fluorobut-3-enoic acid

-
i.e. 3-fluorovinylglycine, irreversible
2-Amino-3-fluorobut-3-enoic acid
-
-
aminooxyacetic acid

-
-
aminooxyacetic acid
-
1 mM, complete inhibition
beta,beta,beta-trifluoroalanine

-
nucleophilic attack of Lys38 on the electrophilic beta-difluoro-alpha,beta-unsaturated imine
beta,beta,beta-trifluoroalanine
-
-
beta,beta,beta-trifluoroalanine
-
nucleophilic attack of Lys38 on the electrophilic beta-difluoro-alpha,beta-unsaturated imine
cycloserine

-
8 microg/ml bacterial culture extract markedly inhibits alanine racemase
cycloserine
-
suicide inhibitor
cycloserine
-
D-cycloserine or a racemic mixture of D- and L-cycloserine
cycloserine
-
D-cycloserine or a racemic mixture of D- and L-cycloserine
D-Chloroalanine

-
Ki: 0.005 mM, competitive
D-cycloserine

-
D-cycloserine
-
an alanine racemase inhibitor
D-cycloserine
-
time-dependent inactivation rate of enzyme from Streptomyces lavendulae is slower than for enzyme from Escherichia coli
D-cycloserine
-
model for inactivation mechanism via geminal diamine and ketimine to isoxazole
D-cycloserine
-
mechanism of inactivation and comparison with inactivation of Streptomyces lavendulae enzyme
D-cycloserine
-
specific inhibition is reversible by D-alanine in the growth medium
D-cycloserine
-
1 mM, 95% inhibition
D-cycloserine
time-dependent inactivation rate of enzyme from Streptomyces lavendulae is slower than for enzyme from Escherichia coli. Enzyme from Streptomyces lavendulae is one of its self-resistance determinants
D-cycloserine
-
mechanism of inactivation and comparison with inactivation of Bacillus stearothermophilus enzyme
hydroxylamine

-
1 mM, 68% inhibition
hydroxylamine
-
non-competitive inhibition kinetics
hydroxylamine
-
1 mM, complete inhibition, both directions
hydroxylamine
-
1 mM, complete inhibition
L-chloroalanine

-
Ki: 1.71 mM, noncompetitive
L-Cycloserine

-
-
L-Cycloserine
-
model for inactivation mechanism via geminal diamine and ketimine to isoxazole
L-Cycloserine
-
mechanism of inactivation and comparison with inactivation of Streptomyces lavendulae enzyme
L-Cycloserine
-
1 mM, 90% inhibition
L-Cycloserine
-
mechanism of inactivation and comparison with inactivation of Bacillus stearothermophilus enzyme
NaCl

-
slight inhibition above 600 mM
NaCl
-
at concentrations around seawater level
phenylhydrazine

-
-
phenylhydrazine
-
1 mM, 72% inhibition
propionate

-
propionate influences both Km (affinity for substrate) and Vmax (enzyme catalysis)
pyridoxal 5'-phosphate

-
slight activation at low concentrations, inhibition at high concentrations
pyridoxal 5'-phosphate
-
0.4 mM, 51% inhibition
Sodium borohydride

-
1 mM, 30% inhibition
Sodium borohydride
complete inactivation after dialysis against
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
additional information

the active-site binding pocket, dimer interface and active-site entryway of the enzyme are potential targets for structure-aided inhibitor design, formation of a template for structure-based drug-development efforts targeting the enzyme, overview
-
additional information
not inhibitory: L-cycloserine
-
additional information
-
not inhibitory: L-cycloserine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
18
D-Lysine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
10
D-serine
-
pH 8.2, 37°C
32
L-lysine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
27
L-serine
-
pH 8.2, 37°C
additional information
additional information
-
0.4
D-Ala

-
-
0.5
D-Ala
-
alr gene encoded
1.1
D-Ala
-
23°C, enzyme Alr
1.4
D-Ala
-
23°C, enzyme DadX
2.2
D-Ala
-
D-Ala, dadB encoded enzyme
73.5
D-Ala
-
30°C, pH 8.5
0.25
D-alanine

-
pH 8.2, 37°C
0.304
D-alanine
-
+/-0.034, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.311
D-alanine
-
+/-0.008, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.4
D-alanine
-
pH 8.2, 37°C
0.402
D-alanine
-
+/-0.055, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.439
D-alanine
-
+/-0.080, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.513
D-alanine
-
+/-0.084, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.528
D-alanine
-
+/-0.079, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.592
D-alanine
-
+/-0.085, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.604
D-alanine
-
+/-0.070, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.615
D-alanine
-
+/-0.032, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.7
D-alanine
pH 8.2, 25°C
0.89
D-alanine
pH not specified in the publication, 30°C, recombinant enzyme
1.008
D-alanine
-
+/-0.069, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.4
D-alanine
-
pH 7.6, 37°C, recombinant enzyme
2.3
D-alanine
-
pH 8.0, 30°C, recombinant mutant Y354W
2.6
D-alanine
-
pH 8.0, 30°C, recombinant mutant I222T
2.8
D-alanine
-
pH 8.0, 30°C, recombinant wild-type enzyme
4
D-alanine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
4.2
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
4.7
D-alanine
-
pH 7.4, 30°C
4.7
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
5.6
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
6.1
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
6.2
D-alanine
Vmax 37.9 micromol/min/mg
6.9
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
7.3
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
8.7
D-alanine
-
pH 7.4, 30°C
8.7
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
12
D-alanine
-
Vmax = 0.44 mol/s/kg
20.16
D-alanine
pH 11.0, 70°C, recombinant enzyme
20.4
D-alanine
-
HPLC analysis
0.5
L-Ala

-
-
1.1
L-Ala
-
23°C, enzyme Alr
1.4
L-Ala
-
23°C, enzyme DadX
1.7
L-Ala
-
alr gene encoded
11
L-Ala
-
dadB gene encoded
0.29
L-alanine

-
pH 8.2, 37°C
0.4
L-alanine
-
pH 8.2, 37°C
0.7
L-alanine
pH 8.2, 25°C
1.049
L-alanine
-
+/-0.131, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.401
L-alanine
-
+/-0.209, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.516
L-alanine
-
+/-0.083, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.562
L-alanine
-
+/-0.256, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.993
L-alanine
-
+/-0.269, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
2.057
L-alanine
-
+/-0.038, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
2.77
L-alanine
pH not specified in the publication, 30°C, recombinant enzyme
3.03
L-alanine
-
+/-0.114, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
3.603
L-alanine
-
+/-0.180, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
4.1
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
4.5
L-alanine
-
pH 8.0, 30°C, recombinant mutant Y354W
4.7
L-alanine
-
pH 8.0, 30°C, recombinant mutant I222T
4.8
L-alanine
-
pH 7.6, 37°C, recombinant enzyme
5.1
L-alanine
-
pH 8.0, 30°C, recombinant wild-type enzyme
7.4
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
8.1
L-alanine
-
pH 7.4, 30°C
8.1
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
8.3
L-alanine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
9.3
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
9.8
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
10.34
L-alanine
-
at pH 9.0 and 37°C
17.4
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
18.4
L-alanine
-
pH 7.4, 30°C
18.4
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
29.6
L-alanine
-
Vmax = 1.02 mol/s/kg
43
L-alanine
-
HPLC analysis
100
L-alanine
Vmax 909 micromol/min/mg
additional information
additional information

-
Km values of L-Ala in the presence of urea at various concentrations
-
additional information
additional information
-
Km values of L-Ala in the presence of urea at various concentrations
-
additional information
additional information
-
effect of NaCl on Km-value
-
additional information
additional information
-
Vmax for the racemization (D- to L-alanine and L- to D-alanine) is 87.0 and 84.8 U/mg, respectively.
-
additional information
additional information
-
Vmax 110 micromol/min/mg D-alanine; Vmax 323 micromol/min/mg L-alanine
-
additional information
additional information
-
Vmax 306 U/mg: D-alanine to L-alanine; Vmax 345 U/mg: L-alanine to D-alanine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.5
D-Lysine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
5.5
D-serine
-
pH 8.2, 37°C
4.17
L-lysine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
13.3
L-serine
-
pH 8.2, 37°C
1.6
D-Ala

-
dadB encoded enzyme
2.6
D-Ala
-
alr encoded enzyme
24.8
D-Ala
-
90°C, pH 9.5
2314
D-Ala
-
pH 8.5, 37°C
3270
D-Ala
-
30°C, pH 8.5
3272
D-Ala
-
30°C, pH 8.5
0.06
D-alanine

-
pH 7.6, 37°C, recombinant enzyme
0.333
D-alanine
-
+/-0.033, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.317
D-alanine
-
+/-0.100, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
2 - 8
D-alanine
-
pH 8.2, 37°C
4
D-alanine
-
+/-0.417, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
4.466
D-alanine
-
+/-0.200, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
5.267
D-alanine
-
+/-0.333, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
5.783
D-alanine
-
+/-0.483, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
6.35
D-alanine
-
+/-0.333, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
6.817
D-alanine
-
+/-0.650, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
7.617
D-alanine
-
+/-0.750, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
63.3
D-alanine
-
pH 8.2, 37°C
70
D-alanine
pH 8.2, 25°C
517
D-alanine
-
pH 8.0, 30°C, recombinant mutant Y354W
633
D-alanine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
983
D-alanine
-
pH 8.0, 30°C, recombinant mutant I222T
1017
D-alanine
-
pH 8.0, 30°C, recombinant wild-type enzyme
1.1
L-Ala

-
-
7.3
L-Ala
-
dadB encoded enzyme
9.7
L-Ala
-
alr encoded enzyme
2589
L-Ala
-
pH 8.5, 37°C
7500
L-Ala
-
30°C, pH 8.5
7504
L-Ala
-
30°C, pH 8.5
0.9
L-alanine

-
pH 7.6, 37°C, recombinant enzyme
2.8
L-alanine
-
+/-0.250, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
16.72
L-alanine
-
+/-0.850, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
22.47
L-alanine
-
+/-2.667, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
27.6
L-alanine
-
pH 8.2, 37°C
41.82
L-alanine
-
+/-2.600, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
51.77
L-alanine
-
+/-6.067, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
53.98
L-alanine
-
+/-3.217, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
55
L-alanine
-
pH 8.2, 37°C
55
L-alanine
pH 8.2, 25°C
67.07
L-alanine
-
+/-7.633, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
68.23
L-alanine
-
+/-7.550, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
70.63
L-alanine
-
at pH 9.0 and 37°C
70.92
L-alanine
-
+/-2.333, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1133
L-alanine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W; pH 8.0, 30°C, recombinant mutant Y354W
1417
L-alanine
-
pH 8.0, 30°C, recombinant mutant I222T
1533
L-alanine
-
pH 8.0, 30°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.14
D-Lysine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
0.13
L-lysine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
0.045
D-alanine

-
pH 7.6, 37°C, recombinant enzyme
158.3
D-alanine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
216.7
D-alanine
-
pH 8.0, 30°C, recombinant mutant Y354W
366.7
D-alanine
-
pH 8.0, 30°C, recombinant wild-type enzyme
383.3
D-alanine
-
pH 8.0, 30°C, recombinant mutant I222T
0.038
L-alanine

-
pH 7.6, 37°C, recombinant enzyme
136.7
L-alanine
-
pH 8.0, 30°C, recombinant mutant I222T/Y354W
250
L-alanine
-
pH 8.0, 30°C, recombinant mutant Y354W
300
L-alanine
-
pH 8.0, 30°C, recombinant mutant I222T; pH 8.0, 30°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.086
(4R)-4-amino-3-isoxazolidinone
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.93
2-(4,6-dimethyl-3-oxo-[1,2]thiazolo[5,4-b]pyridin-2-yl)-N-[2-(4-ethoxyphenyl)ethyl]acetamide
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.08
2-phenyl-1-piperidin-1-ylethanethione
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.02
3,3-dihydroxy-1H-quinoline-2,4-dione
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.76
5-chloro-N-(3-chloro-4-methoxyphenyl)-2-(methylsulfonyl)pyrimidine-4-carboxamide
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.68
6-O-[3-chloro-4-(6-methoxycarbonylpyridine-2-carbonyl)oxyphenyl] 2-O-methyl pyridine-2,6-dicarboxylate
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.038
ethyl 3-(pyridin-2-ylthio)propanoate
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.63
N-benzyl-5-chloro-2-methylsulfonylpyrimidine-4-carboxamide
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.33
D-cycloserine

-
mutant Y265F, 37°C, pH 9.1
0.87
D-cycloserine
pH 8.2, 25°C
1.2
D-cycloserine
-
pH 8.2, 25°C
4
D-cycloserine
-
or higher, wild-type, 37°C, pH 9.1
6
L-Cycloserine

-
wild-type, 37°C, pH 9.1
8.2
L-Cycloserine
-
pH 8.2, 25°C
20
propionate

-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.058
(4R)-4-amino-3-isoxazolidinone
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0049
1,1'-(2-oxido-1,2,5-oxadiazole-3,4-diyl)-bis (1-(2-thienyl))-methanone
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0057
2-(2-hydroxyphenoxy)-N-methylacetamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0077
2-(4,6-dimethyl-3-oxo-[1,2]thiazolo[5,4-b]pyridin-2-yl)-N-[2-(4-ethoxyphenyl)ethyl]acetamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0033
2-(4-methoxyphenyl)-1-morpholin-4-ylethanethione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0065
2-(4-methylphenyl)-1-morpholin-4-ylethanethione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0028
2-(hydoxyimino)-6-methyl-2H-benzopyran-3-carboxamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0131
2-(pyridin-3-ylcarbamothioyl sulfanyl)acetic acid
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0016
2-N',2-N',7-N',7-N'-tetramethyl-9H-fluorene-2,7-disulfonohydrazide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.006
2-phenyl-1-piperidin-1-ylethanethione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0052
3,3-dihydroxy-1H-quinoline-2,4-dione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0082
5-chloro-N-(3-chloro-4-methoxyphenyl)-2-(methylsulfonyl)pyrimidine-4-carboxamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.001
6-O-[3-chloro-4-(6-methoxycarbonylpyridine-2-carbonyl)oxyphenyl] 2-O-methyl pyridine-2,6-dicarboxylate
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0026
ethyl 3-(pyridin-2-ylthio)propanoate
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.009
N',N',4-trimethylbenzenesulfonohydrazide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0068
N-benzyl-5-chloro-2-methylsulfonylpyrimidine-4-carboxamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0082
N-hydroxy-2-(2-hydroxyphenoxy)acetamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.5 - 12.5
activity range
7 - 9.5
-
7.0: about 45% of maximal activity, 9.5: about 95% of maximal activity
7.5 - 12.5
-
at pH 7.5 and at pH 12.5 activity is just under 40%, at pH 7 and at pH 13 the enzyme is inactive
9 - 11
-
pH 9: about 50% of maximal activity, pH 11.0: about 35% of maximal activity, racemization from D-Ala to L-Ala
7 - 11

-
pH 7.0: about 75% of maximal activity, pH 11.0: about 75% of maximal activity
7 - 11
-
pH 7.0: about 40% of maximal activity in formation of D-Ala, about 50% of maximal activity in formation of L-Ala, pH 11: about 95% of maximal activity in formation of L-Ala and D-Ala
8.5 - 11

pH 8.5: 35% of max. activity, pH 11: 8% of max. activity, dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase; pH 8.5: 42% of max. activity, pH 11: 58% of max. activity, yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
8.5 - 11
-
pH 8.5: about 55% of maximal activity, pH 11.0: about 65% of maximal activity, racemization from L-Ala to D-Ala
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0 - 70
-
between 20 to 50°C the enzyme activity is 75-100%, at 0°C activity is about 28% and at 70°C activity is 20%
0 - 60
about 30% of maximal activity at 0°C and at 60°C, in absence of pyridoxal 5'-phosphate
0 - 40
-
0°C: about 25% of maximal activity, 40°C: about 45% of maximal activity
20 - 50
-
20°C: about 60% of maximal activity, 50°C, about 35% of maximal activity
30 - 50
30°C, 45% of maximal activity, 50°C: about 50% of maximal activity, in presence of an excess amount of pyridoxal 5'-phosphate, 0.4 mM
30 - 60
30°C and 60°C: approx. 20% of max. activity, dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
30 - 70
30°C: approx. 25% of max. activity, 70°C: approx. 8% of max. activity, yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
35 - 100
-
35°C: about 75% of maximal activity, 100°C: about 55% of maximal activity
40 - 70
-
40°C: about 60% of maximal activity, 70°C: about 50% of maximal activity
25 - 50

-
25°C: about 65% of maximal activity, formation of L-Ala or D-Ala, 50°C: about 50% of maximal activity in formation of D-Ala, about 60% of maximal activity in formation of L-Ala
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.