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Literature summary for 5.1.2.1 extracted from

  • Rankin, J.A.; Mauban, R.C.; Fellner, M.; Desguin, B.; McCracken, J.; Hu, J.; Varganov, S.A.; Hausinger, R.P.
    Lactate racemase nickel-pincer cofactor operates by a proton-coupled hydride transfer mechanism (2018), Biochemistry, 57, 3244-3251 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum F9USS9
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-
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 F9USS9
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-

Reaction

Reaction Comment Organism Reaction ID
(S)-Lactate = (R)-lactate the enzyme does not follow a proton-coupled electron transfer mechanism, but a proton-coupled hydride transfer (PCHT) mechanism. The nickel-pincer cofactor facilitates a proton-coupled hydride transfer (PCHT) mechanism during LarA-catalyzed lactate racemization Lactiplantibacillus plantarum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate
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Lactiplantibacillus plantarum (R)-lactate
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r
(S)-lactate
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Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 (R)-lactate
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r

Synonyms

Synonyms Comment Organism
LARa
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Lactiplantibacillus plantarum

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme contains an organometallic cofactor with nickel coordinated to a covalently tethered pincer ligand, pyridinium-3-thioamide-5-thiocarboxylic acid mononucleotide. The nickel-pincer cofactor facilitates a proton-coupled hydride transfer (PCHT) mechanism during LarA-catalyzed lactate racemization Lactiplantibacillus plantarum

General Information

General Information Comment Organism
additional information 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 Lactiplantibacillus plantarum