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IUBMB Comments This enzyme, found in Lactobacillus plantarum , is involved in the biosynthesis of a nickel-pincer cofactor. The process starts when one enzyme molecule adenylates pyridinium-3,5-dicarboxylate mononucleotide (P2CMN) and covalently binds the adenylated product to an intrinsic cysteine residue. Next, the enzyme cleaves the carbon-sulfur bond, liberating pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide (PCTMN) and leaving a 2-aminoprop-2-enoate (dehydroalanine) residue attached to the protein. Since the cysteine residue is not regenerated in vivo , the enzyme is inactivated during the process. A second enzyme molecule then repeats the process with PCTMN, adenylating it and covalently binding it to the same cysteine residue, followed by liberation of pyridinium-3,5-bisthiocarboxylate mononucleotide (P2TMN) and the inactivation of the second enzyme molecule. cf . EC 4.4.1.45 , extrinsic cysteine-dependent pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase.
The expected taxonomic range for this enzyme is: Lactiplantibacillus plantarum
Reaction Schemes
[LarE]-L-cysteine
+
+
=
[LarE]-dehydroalanine
+
+
+
[LarE]-L-cysteine
+
+
=
[LarE]-dehydroalanine
+
+
+
Synonyms LarE, P2CMN sulfurtransferase, P2TMN synthase, pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase, pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase, more
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P2CMN sulfurtransferase
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ambiguous
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P2TMN synthase
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ambiguous
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pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase
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ambiguous
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pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase
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ambiguous
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LarE
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ambiguous
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1-(5-O-phospho-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl adenylate + [LarE]-L-cysteine = AMP + [LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine
(2b)
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5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl adenylate + [LarE]-L-cysteine = AMP + [LarE]-S-[5-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl]-L-cysteine
(1b)
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ATP + pyridin-1-ium-3,5-dicarboxylate mononucleotide = diphosphate + 5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl adenylate
(1a)
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ATP + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide = diphosphate + 1-(5-O-phospho-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl adenylate
(2a)
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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
(1), overall reaction
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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
(2), overall reaction
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[LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine = [LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide
(2c)
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[LarE]-S-[5-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl]-L-cysteine = [LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide
(1c)
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[LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine pyridin-1-ium-3,5-dicarbothioate-mononucleotide-lyase (ATP-consuming)
This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. The process starts when one enzyme molecule adenylates pyridinium-3,5-dicarboxylate mononucleotide (P2CMN) and covalently binds the adenylated product to an intrinsic cysteine residue. Next, the enzyme cleaves the carbon-sulfur bond, liberating pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide (PCTMN) and leaving a 2-aminoprop-2-enoate (dehydroalanine) residue attached to the protein. Since the cysteine residue is not regenerated in vivo, the enzyme is inactivated during the process. A second enzyme molecule then repeats the process with PCTMN, adenylating it and covalently binding it to the same cysteine residue, followed by liberation of pyridinium-3,5-bisthiocarboxylate mononucleotide (P2TMN) and the inactivation of the second enzyme molecule. cf. EC 4.4.1.45, extrinsic cysteine-dependent pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase.
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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
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
additional information
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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
Substrates: - Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
-
Substrates: overall reaction Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
-
Substrates: overall reaction Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
additional information
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Substrates: the enzyme activates the lactate racemase LarA Products: -
?
additional information
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Substrates: the enzyme activates the lactate racemase LarA Products: -
?
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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
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
additional information
?
-
[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
-
Substrates: overall reaction Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
-
Substrates: overall reaction Products: -
?
[LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP
[LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
Substrates: - Products: -
?
additional information
?
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Substrates: the enzyme activates the lactate racemase LarA Products: -
?
additional information
?
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Substrates: the enzyme activates the lactate racemase LarA Products: -
?
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ATP
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Ni2+
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the enzyme contains 0.8 mol Ni2+ mol protein-1
Mg2+
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required in form of Mg-ATP
Mg2+
required in form of Mg-ATP
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
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the enzyme, LarE, when expressed in the presence of the other two other accessory proteins LarB and LarC, is able to activate the LarA apoprotein in vitro
metabolism
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the enzyme is required in the lactate racemase system
metabolism
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the enzyme is required in the lactate racemase system
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LARE_LACPL
Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
276
0
30484
Swiss-Prot
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?
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x * 31550, calculated from amino acid sequence
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hanging drop vapor diffusion method, using 105 mM ammonium sulfate, 50 mM bis-Tris pH 6.5, 37.5 % (v/v) pentaerythritol ethoxylate
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D30A
inactive
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Strep-tactin column chromatography and Superdex 200 gel filtration
Strep-Tactin column chromatography, and Superdex 200 gel filtration
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Strep-tactin column chromatography and Superdex 200 gel filtration
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Strep-tactin column chromatography and Superdex 200 gel filtration
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expressed in Lactococcus lactis
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expressed in Lactococcus lactis and Escherichia coli Arctic-Express (DE3) cells
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Desguin, B.; Goffin, P.; Viaene, E.; Kleerebezem, M.; Martin-Diaconescu, V.; Maroney, M.; Declercq, J.; Soumillion, P.; Hols, P.
Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system
Nat. Commun.
5
3615
2014
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum NCIMB 8826
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Desguin, B.; Soumillion, P.; Hols, P.; Hausinger, R.
Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion
Proc. Natl. Acad. Sci. USA
113
5598-5603
2016
Lactiplantibacillus plantarum
brenda
Desguin, B.; Soumillion, P.; Hols, P.; Hu, J.; Hausinger, R.
Lactate racemase and its niacin-derived, covalently-tethered, nickel cofactor
RSC Metallobiol.
2017
220-236
2017
Lactiplantibacillus plantarum
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brenda
Fellner, M.; Desguin, B.; Hausinger, R.; Hu, J.
Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE
Proc. Natl. Acad. Sci. USA
114
9074-9079
2017
Lactiplantibacillus plantarum (F9UST4), Lactiplantibacillus plantarum ATCC BAA-793 (F9UST4)
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