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Information on EC 4.99.1.12 - pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase and Organism(s) Lactiplantibacillus plantarum and UniProt Accession F9UST1

for references in articles please use BRENDA:EC4.99.1.12
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IUBMB Comments
This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. It catalyses the insertion of Ni2+ into the cofactor forming a covalent bond between a carbon atom and the nickel atom.
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This record set is specific for:
Lactiplantibacillus plantarum
UNIPROT: F9UST1
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The taxonomic range for the selected organisms is: Lactiplantibacillus plantarum
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
LarC, P2TMN nickel chelatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LarC
-
-
-
-
P2TMN nickel chelatase
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide nickel-lyase (pyridinium-3,5-bisthiocarboxylate-mononucleotide forming)
This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. It catalyses the insertion of Ni2+ into the cofactor forming a covalent bond between a carbon atom and the nickel atom.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide
pyridinium-3,5-bisthiocarboxylate mononucleotide + Ni2+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide
pyridinium-3,5-bisthiocarboxylate mononucleotide + Ni2+
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55000, Strep-tagged enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Lactococcus lactis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (F9UST1), Lactiplantibacillus plantarum NCIMB 8826 (F9UST1)
Manually annotated by BRENDA team
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 (F9UST1)
Manually annotated by BRENDA team
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 (F9UST1)
Manually annotated by BRENDA team