5.1.2.1: lactate racemase
This is an abbreviated version!
For detailed information about lactate racemase, go to the full flat file.
Word Map on EC 5.1.2.1
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5.1.2.1
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lactobacillus
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plantarum
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racemization
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pincer
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hydride
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organometallic
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nickel-containing
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proton-coupled
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nife-hydrogenase
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sacrificial
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insertase
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ni-dependent
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sakei
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pyridinium
- 5.1.2.1
- lactobacillus
- plantarum
-
racemization
-
pincer
-
hydride
-
organometallic
-
nickel-containing
-
proton-coupled
- nife-hydrogenase
-
sacrificial
-
insertase
-
ni-dependent
- sakei
-
pyridinium
Reaction
Synonyms
Hydroxyacid racemase, lactate racemase, Lactic acid racemase, Lacticoracemase, LAR, LARa, nickel-dependent lactate racemase, Racemase, lactate
ECTree
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General Information
General Information on EC 5.1.2.1 - lactate racemase
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evolution
malfunction
physiological function
additional information
analysis of the lar gene cluster and its encoded Lar proteins, phylogenetic tree. 92% of the genomes bearing a larA homologue (102 out of 111 genomes) also contain the genes for the Lar accessory proteins (larBCE), further reinforcing the necessity of these proteins for LarA activation
evolution
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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analysis of the lar gene cluster and its encoded Lar proteins, phylogenetic tree. 92% of the genomes bearing a larA homologue (102 out of 111 genomes) also contain the genes for the Lar accessory proteins (larBCE), further reinforcing the necessity of these proteins for LarA activation
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disruption of the operon encoding lactate racemase (larA-E), which catalyzes the interconversion between D- and L-latate, completely abolishes D-lactate production. An engineered Lactobacillus plantarum strain lacking the enzyme is useful in the production of L-lactate from starchy materials
malfunction
mutations in the Lar box strongly affect LarR binding and completely abolish transcription from the larA promoter (PlarA)
malfunction
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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disruption of the operon encoding lactate racemase (larA-E), which catalyzes the interconversion between D- and L-latate, completely abolishes D-lactate production. An engineered Lactobacillus plantarum strain lacking the enzyme is useful in the production of L-lactate from starchy materials
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malfunction
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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mutations in the Lar box strongly affect LarR binding and completely abolish transcription from the larA promoter (PlarA)
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lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system. Four proteins and Ni are required for in vivo Lar activity. Necessity of the Lar accessory proteins (larBCE), for LarA activation. Ni-loaded LarE acts as a maturation protein responsible for the activation of apo-LarA, and indicate that LarB and LarC are involved in the activation of LarE prior to apo-LarA activation
physiological function
lactic acid racemization is involved in lactate metabolism and cell wall assembly of many microorganisms
physiological function
the lactate racemase is a nickel-dependent enzyme requiring activation by the accessory protein LarE, which itself requires activation by the accessory proteins LarB and LarC and nickel. The interconversion of lactate isomers is performed by a lactate racemase (Lar) that is transcriptionally controlled by the L-/D-lactate ratio and maximally induced in the presence of L-lactate. The Lar activity depends on the expression of two divergently oriented operons: (i) the larABCDE operon encodes the nickel-dependent lactate racemase (LarA), its maturases (LarBCE), and a lactic acid channel (LarD), and (ii) the larR(MN)QO operon encodes a transcriptional regulator (LarR) and a four-component ABC-type nickel transporter [Lar(MN), in which the M and N components are fused, LarQ, and LarO]. LarR is a regulator of the Crp-Fnr family (PrfA group). L-Lactate has a positive effect on the binding and multimerization of LarR, while D-lactate antagonizes the positive effect of L-lactate. A possible mechanism of LarR regulation by lactate enantiomers is proposed. Hypothetical model of PlarA regulation by LarR: in the presence of L-lactate, activated LarR binds to the Lar box motif and multimerizes on the half-Lar boxes. This will promote direct interaction of one LarR dimer with the RNA polymerase, resulting in transcriptional activation of the PlarA (productive binding). In the presence of D-lactate, D-lactatet can block LarR activation, for instance, by impairing L-lactate recognition, which will result in limited LarR binding and multimerization and absence of transcriptional activation (unproductive binding). Role of LarR in vivo and in vitro
physiological function
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
-
lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system. Four proteins and Ni are required for in vivo Lar activity. Necessity of the Lar accessory proteins (larBCE), for LarA activation. Ni-loaded LarE acts as a maturation protein responsible for the activation of apo-LarA, and indicate that LarB and LarC are involved in the activation of LarE prior to apo-LarA activation
-
physiological function
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
-
the lactate racemase is a nickel-dependent enzyme requiring activation by the accessory protein LarE, which itself requires activation by the accessory proteins LarB and LarC and nickel. The interconversion of lactate isomers is performed by a lactate racemase (Lar) that is transcriptionally controlled by the L-/D-lactate ratio and maximally induced in the presence of L-lactate. The Lar activity depends on the expression of two divergently oriented operons: (i) the larABCDE operon encodes the nickel-dependent lactate racemase (LarA), its maturases (LarBCE), and a lactic acid channel (LarD), and (ii) the larR(MN)QO operon encodes a transcriptional regulator (LarR) and a four-component ABC-type nickel transporter [Lar(MN), in which the M and N components are fused, LarQ, and LarO]. LarR is a regulator of the Crp-Fnr family (PrfA group). L-Lactate has a positive effect on the binding and multimerization of LarR, while D-lactate antagonizes the positive effect of L-lactate. A possible mechanism of LarR regulation by lactate enantiomers is proposed. Hypothetical model of PlarA regulation by LarR: in the presence of L-lactate, activated LarR binds to the Lar box motif and multimerizes on the half-Lar boxes. This will promote direct interaction of one LarR dimer with the RNA polymerase, resulting in transcriptional activation of the PlarA (productive binding). In the presence of D-lactate, D-lactatet can block LarR activation, for instance, by impairing L-lactate recognition, which will result in limited LarR binding and multimerization and absence of transcriptional activation (unproductive binding). Role of LarR in vivo and in vitro
-
physiological function
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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lactic acid racemization is involved in lactate metabolism and cell wall assembly of many microorganisms
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electron paramagnetic resonance spectroscopy of LarA in the absence or presence of substrate revealing a +2 metal oxidation state and inconsistent with a previously proposed proton-coupled electron transfer mechanism. Computational modeling supports hydride transfer to the cofactor at the C4 position or to the nickel atom, but with formation of a nickel-hydride species requiring dissociation of the His200 metal ligand
additional information
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electron paramagnetic resonance spectroscopy of LarA in the absence or presence of substrate revealing a +2 metal oxidation state and inconsistent with a previously proposed proton-coupled electron transfer mechanism. Computational modeling supports hydride transfer to the cofactor at the C4 position or to the nickel atom, but with formation of a nickel-hydride species requiring dissociation of the His200 metal ligand
additional information
LarA catalytic site structure analysis in subunits one and two, overview. Structure comparisons to LarA from Thermus thermophilus
additional information
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LarA catalytic site structure analysis in subunits one and two, overview. Structure comparisons to LarA from Thermus thermophilus
additional information
the active-site structure is constructed from chain B of the recent crystal structure of Lactobacillus plantarum LarA, PDB ID 5HUQ
additional information
the wide distribution of the accessory proteins without Lar
additional information
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the wide distribution of the accessory proteins without Lar
additional information
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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LarA catalytic site structure analysis in subunits one and two, overview. Structure comparisons to LarA from Thermus thermophilus
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additional information
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
-
electron paramagnetic resonance spectroscopy of LarA in the absence or presence of substrate revealing a +2 metal oxidation state and inconsistent with a previously proposed proton-coupled electron transfer mechanism. Computational modeling supports hydride transfer to the cofactor at the C4 position or to the nickel atom, but with formation of a nickel-hydride species requiring dissociation of the His200 metal ligand
-
additional information
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
-
the active-site structure is constructed from chain B of the recent crystal structure of Lactobacillus plantarum LarA, PDB ID 5HUQ
-
additional information
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
-
the wide distribution of the accessory proteins without Lar
-