5.1.1.1: alanine racemase
This is an abbreviated version!
For detailed information about alanine racemase, go to the full flat file.
Word Map on EC 5.1.1.1
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5.1.1.1
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pyridoxal
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5'-phosphate
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peptidoglycan
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racemization
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d-cycloserine
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stearothermophilus
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plp-dependent
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d-amino
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aldimine
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d-alanyl-d-alanine
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exosporium
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pyridoxal-5'-phosphate-dependent
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drug development
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5'-phosphate-dependent
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d-alanine:d-alanine
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medicine
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biotechnology
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pharmacology
- 5.1.1.1
- pyridoxal
- 5'-phosphate
- peptidoglycan
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racemization
- d-cycloserine
- stearothermophilus
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plp-dependent
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d-amino
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aldimine
- d-alanyl-d-alanine
- exosporium
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pyridoxal-5'-phosphate-dependent
- drug development
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5'-phosphate-dependent
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d-alanine:d-alanine
- medicine
- biotechnology
- pharmacology
Reaction
Synonyms
1SFT, AAR, alanine racemase, AlaR, ALR, alr-2, ALR1, ALR2, Alr2 racemase, AlrA, AlrAba, AlrBax, AlrMtb, alrTt, ARL, BA0252, BAS0238, CBL/ALR, CdAlr, cystathionine beta-lyase, D-alanine racemase, DadB, DadX, dadXOF4, dal1, EcAlr, EcCBL, EfAlaR, L-Alanine racemase, L-Alanine:D-alanine racemase, MBalr1, MBAlr2, MetC, More, MurI, OEOE_1641, PDB, Racemase, alanine, tAlaRac, TmCBL, wMelCBL
ECTree
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Engineering
Engineering on EC 5.1.1.1 - alanine racemase
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D318K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
D43K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
D70K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
E134K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
E71K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
D318K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
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D43K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
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D70K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
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E134K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
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E71K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
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deltaalr
Q81VF6
mutant with knocked out alanine racemase gene alr (2 alanine racemase-genes have been found in Bacillus anthracis jet)
Q360A
site-directed mutagenesis, the mutant shows about 1.2fold increased activity compared to the wild-type enzyme
Q360C
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Q360D
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Q360E
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Q360F
site-directed mutagenesis, the mutant shows about 1.5fold increased activity compared to the wild-type enzyme
Q360G
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360H
site-directed mutagenesis, the mutant shows about 2.4fold increased activity compared to the wild-type enzyme
Q360I
site-directed mutagenesis, the mutant shows 3fold increased activity compared to the wild-type enzyme
Q360K
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Q360L
site-directed mutagenesis, the mutant shows about 2.5fold increased activity compared to the wild-type enzyme
Q360M
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360N
site-directed mutagenesis, the mutant shows about 2.3fold increased activity compared to the wild-type enzyme
Q360P
site-directed mutagenesis, the mutant shows about 1.5fold increased activity compared to the wild-type enzyme
Q360R
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360S
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360T
site-directed mutagenesis, the mutant shows about 1.8fold increased activity compared to the wild-type enzyme
Q360V
site-directed mutagenesis, the mutant shows about 2.3fold increased activity compared to the wild-type enzyme
Q360W
site-directed mutagenesis, the mutant shows 3fold increased activity compared to the wild-type enzyme
Q360Y
site-directed mutagenesis, the mutant shows 3fold increased activity compared to the wild-type enzyme
S171A/H359Y
site-directed mutagenesis
K39A
D164A
alanine racemase Alr from Escherichia coli with single point mutation from D to A at position 164
D164K
alanine racemase Alr from Escherichia coli with single point mutation from D to K at position 164
E165A
alanine racemase Alr from Escherichia coli with single point mutation from E to A at position 165
E165K
alanine racemase Alr from Escherichia coli with single point mutation from E to K at position 165
E221A
alanine racemase Alr from Escherichia coli with single point mutation from E to A at position 221
E221K
alanine racemase Alr from Escherichia coli with single point mutation from E to K at position 221
E221P
alanine racemase Alr from Escherichia coli with single point mutation from E to P at position 221
P219A
alanine racemase Alr from Escherichia coli with single point mutation from P to A at position 219
I222T
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
I222T/Y354W
site-directed mutagenesis, the double mutant is an alanine racemase with lysine racemization activity
K39A
R219E
catalytical active mutant, the catalytic effect in the Arg219Glu mutant enzyme is due to a combined solvent and inherent stabilizing effect of the protonated cofactor, in contrast to the wild-type enzyme where the catalytic effect may be ascribed to solvent effects alone
Y265A
Lys39 is the catalytic residue required for the abstraction and addition of the alpha-hydrogen of D-alanine, As shown by site-directed mutagenesis (K39A mutant) and chemical rescue studies. Tyr265 is catalytic residue for L-alanine, shown by site-directed mutagenesis (Y265A mutant)
Y354W
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
A131K
M319T
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the M319T mutation is positioned close enough to allow interaction with the D-cycloserine moiety, which, given the large change of the character of the side chain, can strongly affect D-cycloserine reactivity. M319 is located near Y364 and, as a result, it is possible that the M319T mutation alters the interaction with Y364, thereby affecting D-cycloserine inhibition. The M319T mutant enzyme shows minimal inhibition by D-cycloserine, even at 1 mM, the IC50 of this mutant cannot be determined
R373L
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the mutation is not directly located within the active site but near the dimer interface and close to residues M319 and D320, which play an important role in the makeup of the active site. The replacement of arginine with the short and hydrophobic side chain of leucine might disrupt molecular interactions at the dimer interface as well as destabilize the DCS binding site. The R373L mutation is not located directly within the active site, but also showa a significant increase in resistance to D-cycloserine, with an 27fold increased IC50 compared to the wild-type enzyme
Y364D
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the mutation to aspartic acid introduces a shorter and negatively charged side chain, which potentially affects pyridoxal 5'-phosphate orientation in the active site. The IC50 of the Y364D mutant for D-cycloserine shows a 50fold increase compared to the wild-type
additional information
site-directed mutagenesis, kinetically inactive mutant, the mutation disrupts the binding of the cofactor that is essential for catalysis (pyridoxal 5'-phosphate), the mutant shows altered binding kinetics with L-alanine and D-alanine, weak binding to L- and D-serine
K39A
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site-directed mutagenesis, kinetically inactive mutant, the mutation disrupts the binding of the cofactor that is essential for catalysis (pyridoxal 5'-phosphate), the mutant shows altered binding kinetics with L-alanine and D-alanine, weak binding to L- and D-serine
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mutant enzyme is inactive as a catalyst for racemization as well as transamination
K39A
Lys39 is the catalytic residue required for the abstraction and addition of the alpha-hydrogen of D-alanine, As shown by site-directed mutagenesis (K39A mutant) and chemical rescue studies. Tyr265 is catalytic residue for L-alanine, shown by site-directed mutagenesis (Y265A mutant)
site-directed mutagenesis, the mutant shows a 3fold increased activity compared to wild-type
A131K
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site-directed mutagenesis, the mutant shows a 3fold increased activity compared to wild-type
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enzyme residue Gln360 and conformational changes of active site residues disrupt the hydrogen bonding interactions necessary for proper pyridoxal 5'-phosphate immobilization, and decrease both the substrate affinity and turnover number of AlrTt. Introduction of hydrophobic amino acids at Gln360 increase the racemase activity of AlrTt
additional information
construction of a alr2 knockout mutant RS07 generated by retargeting the pJS107 TargeTron plasmid. Complementation by expression of plasmid pRS89 encoding gene alr2. The alr2 mutant spores more readily germinate in response to L-alanine as a co-germinant, D-alanine also functions as a co-germinant, no germination in presence of taurocholic acid
additional information
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construction of a alr2 knockout mutant RS07 generated by retargeting the pJS107 TargeTron plasmid. Complementation by expression of plasmid pRS89 encoding gene alr2. The alr2 mutant spores more readily germinate in response to L-alanine as a co-germinant, D-alanine also functions as a co-germinant, no germination in presence of taurocholic acid
additional information
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construction of a alr2 knockout mutant RS07 generated by retargeting the pJS107 TargeTron plasmid. Complementation by expression of plasmid pRS89 encoding gene alr2. The alr2 mutant spores more readily germinate in response to L-alanine as a co-germinant, D-alanine also functions as a co-germinant, no germination in presence of taurocholic acid
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additional information
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DNA shuffling of enzyme genes from Salmonella typhimurium and Escherichia coli selecting clones that exhibit higher catalytic activity toward alanine as well as serine. Specific activities of selected clones were increased up to three times more than of wild types. One mutant achieves posttranslationally a high protein level
additional information
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mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
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mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
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mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
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in-frame deletion mutation, loss of ability to grow on D-alanine
additional information
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double mutant for the alr encoded enzyme and the dad B encoded enzyme display a phenotype of requirement for exogenous D-Ala for growth
additional information
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double mutant for the alr encoded enzyme and the dad B encoded enzyme display a phenotype of requirement for exogenous D-Ala for growth
additional information
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DNA shuffling of enzyme genes from Salmonella typhimurium and Escherichia coli selecting clones that exhibit higher catalytic activity toward alanine as well as serine. Specific activities of selected clones were increased up to three times more than of wild types. One mutant achieves posttranslationally a high protein level
additional information
construction of an alr mutant strain. D-Ala starvation causes cell morphology alterations of the alr mutant
additional information
upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Phenotype, overview. Decreased cariogenicity of alr-mutant strain in rats
additional information
Streptococcus mutans serotype c ATCC 700610 / UA159
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construction of an alr mutant strain. D-Ala starvation causes cell morphology alterations of the alr mutant
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additional information
Streptococcus mutans serotype c ATCC 700610 / UA159
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upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Phenotype, overview. Decreased cariogenicity of alr-mutant strain in rats
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