Information on EC 6.3.5.10 - adenosylcobyric acid synthase (glutamine-hydrolysing)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
6.3.5.10
-
RECOMMENDED NAME
GeneOntology No.
adenosylcobyric acid synthase (glutamine-hydrolysing)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O = 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosylcobalamin biosynthesis from cobyrinate a,c-diamide I
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adenosylcobalamin biosynthesis from cobyrinate a,c-diamide II
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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vitamin B12 metabolism
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SYSTEMATIC NAME
IUBMB Comments
adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase (ADP-forming)
Requires Mg2+. NH3 can act instead of glutamine. This enzyme catalyses the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates.
CAS REGISTRY NUMBER
COMMENTARY hide
137672-90-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
strains NRC-1 and MPK414
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Manually annotated by BRENDA team
strain SC510 Rifr(pXL617)
SwissProt
Manually annotated by BRENDA team
strain TR6583
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
show the reaction diagram
ATP + adenosylcobyrinic acid a,c-diamide + ammonia + H2O
ADP + phosphate + adenosylcobyric acid + ?
show the reaction diagram
-
ammonia can replace L-glutamine as amide group donor, but L-glutamine is preferred
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-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
show the reaction diagram
ATP + adenosylcobyrinic acid diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
show the reaction diagram
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four carboxylates attached to the corrinoid ring are amidated in a dissociative fashion. The four carboxylates are amidated in a sequence beginning with carboxylate e and followed in turn by carboxylates d, b, and g
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-
?
ATP + adenosylcobyrinic acid pentaamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
show the reaction diagram
ATP + adenosylcobyrinic acid tetraamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
show the reaction diagram
ATP + adenosylcobyrinic acid triamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
show the reaction diagram
cobinic acid a,c-diamide + ATP + L-glutamine + H2O
cobinamide + ADP + phosphate + L-glutamate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
show the reaction diagram
-
vitamin B12 biosynthesis
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00104
adenosylcobyrinic acid a,c-diamide
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pH 7.5
0.0027
adenosylcobyrinic acid diamide
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30C, pH 7.5
0.0007 - 0.00125
adenosylcobyrinic acid pentaamide
0.0008 - 0.00121
adenosylcobyrinic acid tetraamide
0.001 - 0.00122
adenosylcobyrinic acid triamide
20.4
ammonia
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pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate
0.011 - 0.12
ATP
0.033 - 0.064
L-glutamine
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6
adenosylcobyrinic acid diamide
Salmonella enterica subsp. enterica serovar Typhimurium
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30C, pH 7.5
8.4
adenosylcobyrinic acid pentaamide
Salmonella enterica subsp. enterica serovar Typhimurium
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30C, pH 7.5
3.6
adenosylcobyrinic acid tetraamide
Salmonella enterica subsp. enterica serovar Typhimurium
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30C, pH 7.5
2.4
adenosylcobyrinic acid triamide
Salmonella enterica subsp. enterica serovar Typhimurium
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30C, pH 7.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.083
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pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51982
2 * 51982, CobQ sequence calculation, 2 * 57000
52000
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predicted from DNA sequence of the cobQ gene
97300
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% w/v and 1 mM dithiothreitol are necessary to stabilize enzyme during purification
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxidation
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651618
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or 0C, purified enzyme, 0.1 M Tris hydrochloride, pH 7.5, 48 h, 100% loss of activity
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-20C, purified enzyme, 50 mM Tris hydrochloride, pH 7.5, 0.1 M sodium chloride, 1 mM dithiothreitol, 20% glycerol, several weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cbiP gene
cobQ gene, sequencing, genomic organization
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (109 entries)
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