Information on EC 6.3.4.9 - biotin-[methylmalonyl-CoA-carboxytransferase] ligase

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The expected taxonomic range for this enzyme is: Propionibacterium freudenreichii subsp. shermanii

EC NUMBER
COMMENTARY hide
6.3.4.9
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RECOMMENDED NAME
GeneOntology No.
biotin-[methylmalonyl-CoA-carboxytransferase] ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biotin metabolism
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-
Metabolic pathways
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-
SYSTEMATIC NAME
IUBMB Comments
biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-66-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + biocytin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
?
show the reaction diagram
-
-
-
-
-
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
?
show the reaction diagram
-
-
-
-
-
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram
CTP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
CMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram
-
23% of the activity relative to ATP
-
-
-
GTP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
GMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram
-
18% of the activity relative to ATP
-
-
-
ITP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
IMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram
-
5% of the activity relative to ATP
-
-
-
UTP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
UMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram
-
4% of the activity relative to ATP
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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
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
?
show the reaction diagram
-
-
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0017 mM
Ni2+
-
affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0013 mM
Zn2+
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affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0003 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009
1.3S subunit of apotranscarboxylase
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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6.0: about 45% of maximal activity, 8.0: about 20% of maximal activity
6.4 - 7.4
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6.4: about 70% of maximal activity, 7.4: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
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about 30% of maximal activity at 20°C and 60°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
divalent metal is required for storage stability, Mg2+, Mn2+, Co2+, Zn2+, or Ni2+
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loses activity by repeated freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE