Information on EC 3.5.1.90 - adenosylcobinamide hydrolase

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

EC NUMBER
COMMENTARY hide
3.5.1.90
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RECOMMENDED NAME
GeneOntology No.
adenosylcobinamide hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol
show the reaction diagram
; Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosylcobalamin salvage from cobinamide 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
adenosylcobinamide amidohydrolase
Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).
CAS REGISTRY NUMBER
COMMENTARY hide
905988-16-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain NRC-1
UniProt
Manually annotated by BRENDA team
strain NRC-1
UniProt
Manually annotated by BRENDA team
AV19
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Manually annotated by BRENDA team
strain Göl
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the activity is essential for the conversion of adenosylpseudocobalamin into adenosylcobalamin, the cobinamide needed for the catabolism of acetate. The physiological role of CbiZ in Rhodobacter sphaeroides is to remove the lower ligand of adenosylpseudocobalamin so that the cell can replace the lower ligand with 5,6-dimethylbenzimidazole, generating adenosylcobalamin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(CN)2-cobinamide + H2O
adenosylcobyric acid + ?
show the reaction diagram
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?
(CN)2-cobinamide-GDP + H2O
adenosylcobyric acid + ?
show the reaction diagram
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?
(CN)2-cobinamide-P + H2O
adenosylcobyric acid + ?
show the reaction diagram
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?
adenosylcobinamide + H2O
adenosylcobyric acid + (R)-1-aminopropan-2-ol
show the reaction diagram
adenosylpseudocobalamin + H2O
?
show the reaction diagram
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Rhodobacter sphaeroides requires cobalamin to grow on acetate. It has a CbiZ-dependent mechanism for the conversion of pseudocobalamin into cobalamin
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?
adenosylpseudocobalamine + H2O
adenosylcobyric acid + (R)-1-aminopropan-2-ol
show the reaction diagram
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the enzyme uses adenosylpseudocobalamin as a substrate but not adenosylcobalamin
formation of product monitored by HPLC, product not formed in the absence of dithiothreitol
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?
cyanocobalamin + H2O
adenosylcobyric acid + ?
show the reaction diagram
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?
dicyanocobinamide + H2O
?
show the reaction diagram
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 + H2O
adenosylcobyric acid + (R)-1-aminopropan-2-ol
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
not inhibited by KCN
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MgCl2
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activity is enhanced 2.7fold by adding 10 mM MgCl2 to the reaction mixture
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.009
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(CN)2-cobinamide-GDP as substrate; cyanocobalamin as substrate
0.027
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(CN)2-cobinamide-P as substrate
0.07
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pH 10, 50°C, adenosylpseudocobalamide as substrate
2.1
pH 7.5, 37°C, dicyanocobinamide as substrate
6.4
pH 7.5, 37°C, adenosylcobinamide as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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at pH 10, product formation is linear over time up to 15 min with 1 or 2 microg MBP-CbiZ protein in the reaction mixture
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
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monomer, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the CbiZ protein is isolated as a fusion protein with N-terminal maltose-binding protein MBP an His6 tags and overproduced in Escherichia coli BL21 strain. The recombinant protein is purified
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cbiZ gene, overexpression in Escherichia coli
expression in Escherichia coli and Salmonella enterica
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into the plasmid pBAD24
the CbiZ protein is isolated as a fusion protein with N-terminal maltose-binding protein MBP an His6 tags and overproduced in Escherichia coli BL21 strain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (109 entries)
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