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
5.1.1.1 alanine racemaseAdvanced search results
results (
results (Subunits
Subunits on EC 5.1.1.1 - alanine racemase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homodimer
monomer
tetramer
the Escherichia coli CBL tetramer (PDB entry 1CL1) adopts fold type I
additional information
?
x * 40390, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
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x * 40390, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
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?
x * 47000, recombinant His6-tagged enzyme, SDS-PAGE
dimer
Alkalihalophilus pseudofirmus
2 * 41000, gel filtration and dynamic light scattering
dimer
Alkalihalophilus pseudofirmus OF4
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2 * 41000, gel filtration and dynamic light scattering
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dimer
2 * 46000, recombinant His-tagged wild-type enzyme, SDS-PAGE, 2 * 46621, recombinant His-tagged wild-type enzyme, sequence calculation, 2 * 46605, recombinant His-tagged mutant S171A, sequence calculation, 2 * 46647, recombinant double-His-tagged mutant H359Y, sequence calculation
dimer
the Escherichia coli ALR dimer (PDB entry 2RJG) adopts a fold type III
dimer
formed by two crystallographically different monomers, crystallization data
dimer
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formed by two crystallographically different monomers, crystallization data
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dimer
the enzyme exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites, a symmetric head-to-tail homodimer
dimer
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the enzyme exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites, a symmetric head-to-tail homodimer
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dimer
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
homodimer
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
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homodimer
Alkalihalophilus pseudofirmus
enzyme molecular structure analysis, the tertiary structure of DadXOF4 is a homodimer comprised of two monomers that interact in a head-to-tail manner. Each monomer is composed of two domains, an eight-stranded alpha/beta-barrel at the N-terminus and a C-terminal domain essentially composed of beta-strands. The dimer interface of DadXOF4 is formed by five pairs of salt bridges, i.e. Asp43-Lys360', Asp70-Lys2', Glu71-Arg361', Glu134-Arg259', and Asp318-Lys41'
homodimer
Alkalihalophilus pseudofirmus OF4
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enzyme molecular structure analysis, the tertiary structure of DadXOF4 is a homodimer comprised of two monomers that interact in a head-to-tail manner. Each monomer is composed of two domains, an eight-stranded alpha/beta-barrel at the N-terminus and a C-terminal domain essentially composed of beta-strands. The dimer interface of DadXOF4 is formed by five pairs of salt bridges, i.e. Asp43-Lys360', Asp70-Lys2', Glu71-Arg361', Glu134-Arg259', and Asp318-Lys41'
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homodimer
each monomer covers full-length AlrTt (Val1-Lys383), it contains an N-terminal eight-stranded alpha/beta barrel domain (residues 1-244) and a C-terminal extended beta-strand domain (residues 245-383). The active site is located in the center of alpha/beta barrel domain, it is surrounded by parallel beta strands. Two identical monomers associate at the C-terminal beta-strand domain and the alpha/beta barrel domain to form the functional dimer, enzyme structure determination and analysis, active site structure, detailed overview. A hydrophobic patch localizes underneath Gln360 and phosphate group of pyridoxal 5'-phosphate. This hydrophobic patch is conserved both in sequence and conformation among bacterial alanine racemase
homodimer
2 x 43306, recombinant wild-type enzyme, mass spectrometry, 2 * 43279, recombinant mutant enzyme, mass spectrometry
homodimer
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2 x 43306, recombinant wild-type enzyme, mass spectrometry, 2 * 43279, recombinant mutant enzyme, mass spectrometry
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homodimer
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the homodimeric enzyme of 388 residues formed by a head-to-tail association of two monomers. Each monomer is composed of two folded domains: (i) an N-terminal domain formed by the portion 1-240 and (ii) a C-terminal domain with the remaining portion of the monomer (241-388). The N-terminal domain consists of an eight-stranded alpha/beta-barrel, while the C-terminal domain is made up of beta-strands. Molecular dynamics study
homodimer
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2 * 39075, calculated from amino acid sequence
homodimer
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
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2 * 43400, recombinant enzyme, SDS-PAGE
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monomer
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1 * 39000, SDS-PAGE, 1 * 39700, calculated, enzyme shows monomer-dimer equilibrium
monomer
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1 * 39000, SDS-PAGE, 1 * 39800, calculated, enzyme shows monomer-dimer equilibrium
monomer
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1 * 39000, SDS-PAGE, 1 * 39700, calculated, enzyme shows monomer-dimer equilibrium
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monomer
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1 * 39000, SDS-PAGE, 1 * 39800, calculated, enzyme shows monomer-dimer equilibrium
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monomer
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1 * 39044, calculation from nucleotide sequence
monomer
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1 * 42000, SDS-PAGE
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additional information
three-dimensional enzyme structure of the recombinnat His6-tagged enzyme, overview
additional information
the enzyme forms a homodimer with two active sites in which the cofactor pyridoxal 5'-phosphate is bound. Intermolecular interactions, overview
additional information
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the enzyme forms a homodimer with two active sites in which the cofactor pyridoxal 5'-phosphate is bound. Intermolecular interactions, overview
additional information
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the enzyme forms a homodimer with two active sites in which the cofactor pyridoxal 5'-phosphate is bound. Intermolecular interactions, overview
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additional information
enzyme sequence and structure comparisons, overview
additional information
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enzyme sequence and structure comparisons, overview
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additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
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the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
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the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
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the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
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the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
dimer interfaces for the enzyme is 2510 A2
additional information
enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
additional information
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enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
additional information
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
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enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
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additional information
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three-dimensional structure modeling of Tolypocladium inflatum alanine racemase based on the threonine aldolase crystal structure, homology modeling, overview
