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
6.3.5.11 cobyrinate a,c-diamide synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 6.3.5.11 - cobyrinate a,c-diamide synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ATP + (aq)2cobyrinate + 2 L-glutamine + 2 H2O
2 ADP + 2 phosphate + (aq)2cobyrinate a,c-diamide + 2 L-glutamate
-
76% of the initial velocity with cobyrinate
-
-
?
2 ATP + (CN,aq)cobyrinate + 2 L-glutamine + 2 H2O
2 ADP + 2 phosphate + (CN,aq)cobyrinate a,c-diamide + 2 L-glutamate
-
-
-
-
?
2 ATP + cobyrinate + 2 L-glutamine + 2 H2O
2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate
2 ATP + cobyrinate g-monoamide + L-glutamine + 2 H2O
2 ADP + phosphate + cobyrinate c,g-diamide + L-glutamate
-
145% of the initial velocity with cobyrinate
product is 83% cobyrinate c,g-diamide, 17% cobyrinate a,c,g-triamide
-
?
2 ATP + hydrogenobyrinate + 2 L-glutamine + 2 H2O
2 ADP + 2 phosphate + hydrogenobyrinate a,c-diamide + 2 L-glutamate
-
-
-
-
?
ATP + (CN,aq)cobyrinate c-monoamide + L-glutamine + H2O
ADP + phosphate + (CN,aq)cobyrinate a,c-diamide + L-glutamate
-
-
-
-
?
ATP + cobyrinate a-monoamide + L-glutamine + H2O
ADP + phosphate + cobyrinate a,c-diamide + L-glutamate
-
81% of the initial velocity with cobyrinate
product is 100% cobyrinate a,c-diamide
-
?
ATP + cobyrinate c-monoamide + L-glutamine + H2O
ADP + phosphate + cobyrinate a,c-diamide + L-glutamate
-
19% of the initial velocity with cobyrinate
product is 100% cobyrinate a,c-diamide
-
?
ATP + hydrogenobyrinate c-monoamide + L-glutamine + H2O
ADP + phosphate + hydrogenobyrinate a,c-diamide + L-glutamate
-
19% of the initial velocity with cobyrinate
-
-
?
2 ATP + cobyrinate + 2 ammonia + 2 H2O
2 ADP + 2 phosphate + cobyrinate a,c-diamide
-
-
-
-
?
2 ATP + cobyrinate + 2 ammonia + 2 H2O
2 ADP + 2 phosphate + cobyrinate a,c-diamide
-
-
-
-
?
2 ATP + cobyrinate + 2 L-glutamine + 2 H2O
2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate
-
-
-
-
?
2 ATP + cobyrinate + 2 L-glutamine + 2 H2O
2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate
-
-
the hydrolysis of glutamine and the synthesis of the cobyrinic acid a,c-diamide product are uncoupled. CbiA catalyzes the sequential amidation of the c- and a-carboxylate groups of cobyrinic acid via the formation of a phosphorylated intermediate. CbiA catalyzes 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
-
?
additional information
?
-
enzyme catalyzes ATP-dependent formation of the amide group using the ammonia nitrogen produced by the glutaminase domains. The reaction proceeds through a phosphoacyl intermediate, which is then subjected to the nucleophilic attack of the amino nitrogen, which leads to the formation of the amide bond and liberation of phosphate. Enzyme belongs to a family of ATP-dependent enzymes that also includes dethiobiotin synthetase and cobyric acid synthase CobQ. This enzyme family is also related to the MinD family of ATPases involved in regulation of cell division in bacteria and archaea. CobB and CobQ also contain unusual Triad family class I glutamine amidotransferase domains with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad
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-
?
additional information
?
-
-
no further amidation of cobyrinate a,c-diamide and cobyrinate a,c, g-triamide
-
-
?
additional information
?
-
enzyme catalyzes ATP-dependent formation of the amide group using the ammonia nitrogen produced by the glutaminase domains. The reaction proceeds through a phosphoacyl intermediate, which is then subjected to the nucleophilic attack of the amino nitrogen, which leads to the formation of the amide bond and liberation of phosphate. Enzyme belongs to a family of ATP-dependent enzymes that also includes dethiobiotin synthetase and cobyric acid synthase CobQ. This enzyme family is also related to the MinD family of ATPases involved in regulation of cell division in bacteria and archaea. CobB and CobQ also contain unusual Triad family class I glutamine amidotransferase domains with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad
-
-
?
additional information
?
-
-
CbiA is able to hydrolyze glutamine in the absence of the other two substrates. The addition of ATP alone decreases the Km for glutamine by a factor of 2. Cobyrinic acid enhances the kcat for the hydrolysis of glutamine about 2fold and decreases the Km for glutamine by 20fold. The decrease in the Km for glutamine is about 200fold when both ATP and cobyrinic acid are present in the assay solution. There is no change in the Km for glutamine when ADP is added with cobyrinic acid
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-
?
