Ligand [LarE]-L-cysteine
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Basic Ligand Information
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)
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[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP = [LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
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[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP = [LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
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Substrate in Enzyme-catalyzed Reactions (2 results)
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[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP = [LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
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[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP = [LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
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Enzyme Kinetic Parameters
References & Links
Literature References (2)
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Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion
2016
Desguin, B.; Soumillion, P.; Hols, P.; Hausinger, R.
Proc. Natl. Acad. Sci. USA
113
5598-5603
Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE
2017
Fellner, M.; Desguin, B.; Hausinger, R.; Hu, J.
Proc. Natl. Acad. Sci. USA
114
9074-9079
Links to other databases for [LarE]-L-cysteine