Information on EC 2.7.1.156 - adenosylcobinamide kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.156
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RECOMMENDED NAME
GeneOntology No.
adenosylcobinamide kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RTP + adenosylcobinamide = adenosylcobinamide phosphate + RDP [where RTP is either ATP or GTP]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosylcobalamin salvage from cobinamide I
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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
RTP:adenosylcobinamide phosphotransferase
In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. The second branch of the nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by Cob U. The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalysed by EC 2.7.8.26, adenosylcobinamide-GDP ribazoletransferase (CobS), to yield adenosylcobalamin. CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62, adenosylcobinamide-phosphate guanylyltransferase) activities. However, both activities are not required at all times. The kinase activity has been proposed to function only when S. typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin [4].
CAS REGISTRY NUMBER
COMMENTARY hide
169592-51-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosylcobinamide + ATP
adenosylcobinamide phosphate + ADP
show the reaction diagram
adenosylcobinamide + GTP
adenosylcobinamide phosphate + GDP
show the reaction diagram
adenosylcobinamide phosphate + GTP
adenosylcobinamide-GDP + diphosphate
show the reaction diagram
ATP + 2',5'-dideoxyadenosylcobinamide
2',5'-dideoxyadenosylcobinamide phosphate + ADP
show the reaction diagram
ATP + 5'-deoxyadenosylcobinamide
5'-deoxyadenosylcobinamide phosphate + ADP
show the reaction diagram
ATP + 5'-deoxycytosylcobinamide
5'-deoxycytosylcobinamide phosphate + ADP
show the reaction diagram
ATP + 5'-deoxyguanosylcobinamide
5'-deoxyguanosylcobinamide phosphate + ADP
show the reaction diagram
ATP + 5'-deoxyinosylcobinamide
5'-deoxyinosylcobinamide phosphate + ADP
show the reaction diagram
ATP + adenosylcobinamide
adenosylcobinamide phosphate + ADP
show the reaction diagram
dATP + adenosylcobinamide
adenosylcobinamide phosphate + dADP
show the reaction diagram
dGTP + adenosylcobinamide
adenosylcobinamide phosphate + dGDP
show the reaction diagram
-
-
-
?
GTP + adenosylcobinamide
adenosylcobinamide phosphate + GDP
show the reaction diagram
additional information
?
-
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
adenosylcobinamide + ATP
adenosylcobinamide phosphate + ADP
show the reaction diagram
adenosylcobinamide + GTP
adenosylcobinamide phosphate + GDP
show the reaction diagram
adenosylcobinamide phosphate + GTP
adenosylcobinamide-GDP + diphosphate
show the reaction diagram
ATP + adenosylcobinamide
adenosylcobinamide phosphate + ADP
show the reaction diagram
GTP + adenosylcobinamide
adenosylcobinamide phosphate + GDP
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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The cobU mutations all eliminate the ability of the apt-18 deletion mutant to grow on cobinamide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
5'-deoxyadenosylcobinamide
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pH 8.8, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.251
5'-deoxyadenosylcobinamide
Salmonella enterica subsp. enterica serovar Typhimurium
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pH 8.8, 37C
0.191
ATP
Salmonella enterica subsp. enterica serovar Typhimurium
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pH 8.8, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000003
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GTP:kinase specific activity, mutant H46A
0.00000008
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GTP:kinase specific activity, mutant H46N
0.000251
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GTP:kinase specific activity, mutant H45A
0.001166
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GTP:kinase specific activity, wild-type
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9.5
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50% activity retains in this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
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retains 50% activity in this range, temperatures above 60C results in drastic decrease of activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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predicted pI for the denatured protein
7.2
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experimetally determined isoelectric point
7.5
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experimetally determined isoelectric point
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19700
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predicted mass, based on DNA sequence
20000
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amino acid sequence, small polypeptide with 180 amino acids
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
X-ray crystal structure determined by molecular replacement to 2.2 A resolution, crystals grown by the batch method, cocrystallized with GTP and diphosphate, crystals belong to space group P2(1)2(1)2(1) with unit cell dimensions a : 58.4 A, b : 87.8 A, and c : 101.6 A
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X-ray structure determined to 2.3 A resolution, crystals grown by microbatch, enzyme is crystallized in space group C222(1) with unit cell dimensions of a : 96.4 A, b : 114.4 A, and c : 106.7 A
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
substrates provides little protection from inhibition by DTNB
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
in presence of oxygen kinase activity is lost
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644435
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stored under a N2 headspace, retains 98% of its activity for at least 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CobU protein is overproduced and purified. Cells from a 4-liter culture of the overproducing strain are lysed using a French press. After the addition of ammonium sulfate, fast protein liquid chromatography is used to isolate CobU protein from the clarified cell extract in two additional steps, hydrophobic interaction chromatography and dye ligand chromatography. Protein concentration was determined by the Bradford method.
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recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, hydrophobic interaction chromatography on a phenyl resin, and ultrafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
A chromosomal in-frame deletion of the cobU gene is constructed in strain TR6583.
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Chromosomal in-frame deletion mutations are constructed for the cobU gene using linear transformation and moved into strains with the deletion mutation apt-18, which causes strains to synthesize only pseudo-B12 cofactors.
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gene cobU, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H45A/H46A
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site-directed mutagenesis
H45A/H46A
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site-directed mutagenesis
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