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
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Metals Ions
Metals Ions on EC 5.1.2.1 - lactate racemase
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Ni2+
additional information
absolutely required. Lactobacillus plantarum possesses an organometallic nickel-containing prosthetic group. A nicotinic acid mononucleotide derivative is tethered to Lys184 and forms a tridentate pincer complex that coordinates nickel through one metal-carbon and two metal-sulfur bonds, with His200 as another ligand. Nickel-binding site structure and the role of three accessory proteins required for its activation, overview
Ni2+
dependent on, nickel is an essential cofactor, the enzyme contains 19-21% nickel, measured by PAR assays and ICP-AES. The LarA Ni center is coordinated by His residues, a four coordinate square planar nickel center or a five coordinate square pyramidal site
Ni2+
required, the Ni-tethered pincer cofactor in enzyme LarA increases reaction barriers and destabilizes NADH-like pyruvate intermediates, due to the less electrophilic Ni cofactor and to the ring strain in the pyruvate intermediates, the Ni ion decreases the electron affinity of cofactor
model of the assembly of the lactate racemase metallocenter, overview. Enzyme LarA receives Ni2+ from the pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase, LarE (EC 4.4.1.37)
additional information
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model of the assembly of the lactate racemase metallocenter, overview. Enzyme LarA receives Ni2+ from the pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase, LarE (EC 4.4.1.37)