Enzyme

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EC Tree
     4. Lyases
        4.99 Other lyases
            4.99.1 Sole sub-subclass for lyases that do not belong in the other subclasses
ID:4.99.1.12
Description:Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase.
Alternative Name: P2TMN nickel chelatase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.99.1.12
BRENDA Enzyme Link: BRENDA 4.99.1.12
KEGG Enzyme Link: KEGG4.99.1.12
BioCyc Enzyme Link: BioCyc 4.99.1.12
ExPASy Enzyme Link: ExPASy4.99.1.12
EC2PDB Enzyme Link: EC2PDB 4.99.1.12
ExplorEnz Enzyme Link: ExplorEnz 4.99.1.12
PRIAM enzyme-specific profiles Link: PRIAM 4.99.1.12
IntEnz Enzyme Link: IntEnz 4.99.1.12
MEDLINE Enzyme Link: MEDLINE 4.99.1.12
MSA:

4.99.1.12;

Phylogenetic Tree:

4.99.1.12;

Uniprot:
M-CSA:
RHEA:54784 Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide
RULE(radius=1) [OH;+0:1]-[C;H0;+0:2]1=[S+;H0:3]-[Ni-;H0:4]2-[S;H0;+0:5]-[*:6]-[*:7]:[c;H0;+0:8]-2:[*:9]-1>>[Ni+2;H0:4].[O;H0;+0:1]=[C;H0;+0:2](-[SH;+0:3])-[*:9]:[cH;+0:8]:[*:7]-[*:6]-[SH;+0:5]
Reaction
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References

TitleAuthorsDatePubMed ID
Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion.Desguin B, Soumillion P, Hols P, Hausinger RP2016 May 1727114550