6.6.1.2: cobaltochelatase
This is an abbreviated version!
For detailed information about cobaltochelatase, go to the full flat file.
Word Map on EC 6.6.1.2
-
6.6.1.2
-
cbixs
-
megaterium
-
sirohydrochlorin
-
ferrochelatase
-
archaea
-
tetrapyrrole
-
sirohaem
-
uroporphyrinogen
-
macrocycle
-
magnesium
-
histidine-rich
-
haem
-
primordial
-
eubacteria
-
denitrificans
-
precorrin-2
-
mesoporphyrin
-
ferro
- 6.6.1.2
- cbixs
- megaterium
- sirohydrochlorin
-
ferrochelatase
- archaea
- tetrapyrrole
-
sirohaem
- uroporphyrinogen
-
macrocycle
- magnesium
-
histidine-rich
-
haem
-
primordial
- eubacteria
- denitrificans
- precorrin-2
- mesoporphyrin
-
ferro
Reaction
Synonyms
CbiK, CbiXL, cobalt chelatase, cobaltochelatase, CobN-CobST, CobNST, CobN–CobST, gene cobN/gene cobS cobaltochelatase, holocobalamin synthase, hydrogenobyrinic acid a,c-diamide cobaltochelatase
ECTree
Advanced search results
Systematic Name
Systematic Name on EC 6.6.1.2 - cobaltochelatase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming)
This enzyme, which forms part of the aerobic (late cobalt insertion) cobalamin biosynthesis pathway, is a type I chelatase, being heterotrimeric and ATP-dependent. It comprises two components, one of which corresponds to CobN and the other is composed of two polypeptides, specified by cobS and cobT in Pseudomonas denitrificans, and named CobST [1]. Hydrogenobyrinate is a very poor substrate. ATP can be replaced by dATP or CTP but the reaction proceeds more slowly. CobN exhibits a high affinity for hydrogenobyrinate a,c-diamide. The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding. See EC 4.99.1.3, sirohydrochlorin cobaltochelatase, for the cobaltochelatase that participates in the anaerobic cobalamin biosynthesis pathway.