sirohydrochlorin cobaltochelatase | |||||||||
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Identifiers | |||||||||
EC no. | 4.99.1.3 | ||||||||
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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The enzyme sirohydrochlorin cobaltochelatase (EC 4.99.1.3) catalyzes the reaction
In the forward direction of reactions towards cobalamin in anaerobic bacteria, the two substrates of this enzyme are sirohydrochlorin and Co2+; its two products are cobalt-sirohydrochlorin and H+.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming). Other names in common use include CbiK, CbiX, CbiXS, anaerobic cobalt chelatase, cobaltochelatase [ambiguous], and sirohydrochlorin cobalt-lyase (incorrect). This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria such as Salmonella typhimurium and Bacillus megaterium . It has also been identified as the enzyme which inserts nickel into sirohydrochlorin in the biosynthesis of cofactor F430, reaction EC 4.99.1.11. [1]
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1TJN and 2DJ5.
In enzymology, precorrin-6A synthase (deacetylating) (EC 2.1.1.152) is an enzyme that catalyzes the chemical reaction
In enzymology, a precorrin-2 dehydrogenase (EC 1.3.1.76) is an enzyme that catalyzes the chemical reaction
In enzymology, a precorrin-6A reductase (EC 1.3.1.54) is an enzyme that catalyzes the chemical reaction
In enzymology, a precorrin-3B synthase (EC 1.14.13.83) is an enzyme that catalyzes the chemical reaction
In enzymology, a cob(II)yrinic acid a,c-diamide reductase is an enzyme that catalyzes the chemical reaction
The enzyme sirohydrochlorin ferrochelatase (EC 4.99.1.4) catalyzes the following reaction:
The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction
In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) (EC 6.3.5.10) is an enzyme that catalyzes the chemical reaction
Cobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) (EC 6.3.5.9) is an enzyme that catalyzes the chemical reaction
The primary biochemical reaction catalyzed by the enzyme adenosylcobalamin/α-ribazole phosphatase (formerly α-ribazole phosphatase) (EC 3.1.3.73) is
In enzymology, an adenosylcobinamide-phosphate guanylyltransferase is an enzyme that catalyzes the chemical reaction
Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.
F430 is the cofactor (sometimes called the coenzyme) of the enzyme methyl coenzyme M reductase (MCR). MCR catalyzes the reaction EC 2.8.4.1 that releases methane in the final step of methanogenesis:
Uroporphyrinogen-III C-methyltransferase, uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase. This enzyme catalyses the following chemical reaction
Cobalt-precorrin-5B (C1)-methyltransferase (EC 2.1.1.195), cobalt-precorrin-6A synthase, CbiD (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:cobalt-precorrin-5B (C1)-methyltransferase. This enzyme catalyses the following chemical reaction
Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) (EC 2.1.1.196, CbiT) is an enzyme with systematic name S-adenosyl-L-methionine:precorrin-7 C15-methyltransferase (C12-decarboxylating). This enzyme catalyses the following chemical reaction
Adenosylcobinamide-GDP ribazoletransferase is an enzyme with systematic name adenosylcobinamide-GDP:alpha-ribazole ribazoletransferase. This enzyme catalyses the following chemical reaction
Adenosylcobinamide-phosphate synthase is an enzyme with systematic name adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase (ADP-forming). This enzyme catalyses the following chemical reaction
In biochemistry, chelatases are enzymes that catalyze the insertion ("metalation") of naturally occurring tetrapyrroles. Many tetrapyrrole-based cofactors exist in nature including hemes, chlorophylls, and vitamin B12. These metallo cofactors are derived by the reaction of metal cations with tetrapyrroles, which are not ligands per se, but the conjugate acids thereof. In the case of ferrochelatases, the reaction that chelatases catalyze is: