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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

Reaction

L-alanine
=
D-alanine

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

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.1 alanine racemase

Engineering

Engineering on EC 5.1.1.1 - alanine racemase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
-
D43K
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
-
D70K
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
-
E134K
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
-
E71K
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
-
D48A
-
no effect on the enzyme activity
deltaalr
Q81VF6
mutant with knocked out alanine racemase gene alr (2 alanine racemase-genes have been found in Bacillus anthracis jet)
K41A
-
completely inactive
Y270A
-
impaired enzyme activity
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
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
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)
Y265F
1600fold reduction of racemization
Y354W
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
A131K
M319T
-
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
-
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
-
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