2016
DOI: 10.1073/pnas.1600486113
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Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion

Abstract: The lactate racemase enzyme (LarA) of Lactobacillus plantarum harbors a (SCS)Ni(II) pincer complex derived from nicotinic acid. Synthesis of the enzyme-bound cofactor requires LarB, LarC, and LarE, which are widely distributed in microorganisms. The functions of the accessory proteins are unknown, but the LarB C terminus resembles aminoimidazole ribonucleotide carboxylase/mutase, LarC binds Ni and could act in Ni delivery or storage, and LarE is a putative ATP-using enzyme of the pyrophosphatase-loop superfami… Show more

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Cited by 49 publications
(51 citation statements)
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“…As a result, the bound ATP molecule is oriented with the α-phosphate positioned toward the C-terminal domain of LarE, where the substrate P2CMN is supposed to bind. Consistent with the importance of the SGGxDS motif for LarE function, a D30A LarE variant showed that activity was abolished (7).…”
Section: Resultsmentioning
confidence: 52%
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“…As a result, the bound ATP molecule is oriented with the α-phosphate positioned toward the C-terminal domain of LarE, where the substrate P2CMN is supposed to bind. Consistent with the importance of the SGGxDS motif for LarE function, a D30A LarE variant showed that activity was abolished (7).…”
Section: Resultsmentioning
confidence: 52%
“…In the current structural model, the sulfur atom of Cys176 is only 5.1 Å away from the carboxylic acid group of P2CMN (Fig. 7), providing a strong structural basis for the formation of the Cys176-mediated LarE-P2CMN adduct, which has been detected in previous mass spectrometry experiments (7). Still unclear is the question of how the thiol group of Cys176 is activated to act as a nucleophile.…”
Section: Implications Of the Structural Findings On The Catalytic Mecmentioning
confidence: 54%
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“…1). The nickel center is coordinated by an SCS pincer ligand derived from a nicotinic acid mononucleotide, in addition to histidine (200) (5,6). Based on the structure of this active site, it was proposed that the pincer ligand could reversibly capture a hydride from lactate at the carbon atom coordinated to nickel, in a manner similar to nicotinamide adenine dinucleotide in hydride transfer enzymes (Fig.…”
mentioning
confidence: 99%