cobalt chelatase | |||||||||
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Identifiers | |||||||||
EC no. | 6.6.1.2 | ||||||||
CAS no. | 81295-49-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Cobalt chelatase, CobT subunit | |||||||||
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Identifiers | |||||||||
Symbol | CobT | ||||||||
Pfam | PF06213 | ||||||||
InterPro | IPR006538 | ||||||||
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Cobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are ATP, hydrogenobyrinic acid a,c-diamide, Co 2+, and H2O; its four products are ADP, phosphate, cob(II)yrinic acid a,c-diamide, and H+.
The aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway) [2] [3] consists of three subunits, CobT, CobN (InterPro : IPR003672 ) and CobS (InterPro : IPR006537 ).
The macrocycle of vitamin B12 can be complexed with metal via the ATP-dependent reactions in the aerobic pathway (e.g., in Pseudomonas denitrificans ) or via ATP-independent reactions of sirohydrochlorin in the anaerobic pathway (e.g., in Salmonella typhimurium ). [4] [5] The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS are homologous to Mg-chelatase subunits BchH and BchI, respectively. [5] CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus). [5]
This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names in common use include hydrogenobyrinic acid a,c-diamide cobaltochelatase, CobNST, and CobNCobST. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
Methylcobalamin (mecobalamin, MeCbl, or MeB12) is a cobalamin, a form of vitamin B12. It differs from cyanocobalamin in that the cyano group at the cobalt is replaced with a methyl group. Methylcobalamin features an octahedral cobalt(III) centre and can be obtained as bright red crystals. From the perspective of coordination chemistry, methylcobalamin is notable as a rare example of a compound that contains metal–alkyl bonds. Nickel–methyl intermediates have been proposed for the final step of methanogenesis.
Pseudomonas denitrificans is a Gram-negative aerobic bacterium that performs denitrification. It was first isolated from garden soil in Vienna, Austria. It overproduces cobalamin (vitamin B12), which it uses for methionine synthesis and it has been used for manufacture of the vitamin. Scientists at Rhône-Poulenc Rorer took a genetically engineered strain of the bacteria, in which eight of the cob genes involved in the biosynthesis of the vitamin had been overexpressed, to establish the complete sequence of methylation and other steps in the cobalamin pathway.
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