6.3.5.11: cobyrinate a,c-diamide synthase

This is an abbreviated version!
For detailed information about cobyrinate a,c-diamide synthase, go to the full flat file.

Reaction

2 ATP +

Synonyms

CbiA, CobB

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor

                6.3.5.11 cobyrinate a,c-diamide synthase

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Results	in table
8744	AA Sequence
1	Application
3	Cloned(Commentary)
1	General Information
1	Inhibitors
4	kcat/KM [mM/s]
11	KM Value [mM]
5	Molecular Weight [Da]
6	Organism
5	Pathway
2	pH Optimum
8	Protein Variants
1	Purification (Commentary)
4	Reaction
6	Reference
1	Specific Activity [micromol/min/mg]
16	Substrates and Products (Substrate)
2	Subunits
3	Synonyms
1	Systematic Name
4	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 6.3.5.11 - cobyrinate a,c-diamide synthase

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SYSTEMATIC NAME

IUBMB Comments

cobyrinate:L-glutamine amido-ligase (ADP-forming)

This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyses the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source. It is proposed that the enzyme first catalyses the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate. The Km for ammonia is substantially higher than that for L-glutamine. The equivalent reaction in the aerobic cobalamin biosynthesis pathway is catalysed by EC 6.3.5.9, hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing).