Information on EC 6.3.4.9 - Biotin-[methylmalonyl-CoA-carboxytransferase] ligase:
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The lowest common taxonomy group for this enzyme is: Propionibacterium freudenreichii subsp. shermanii

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EC NUMBERCOMMENTARY
6.3.4.9-

RECOMMENDED NAMEGeneOntology No.
Biotin-[methylmalonyl-CoA-carboxytransferase] ligaseGO:0004079

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]
show the reaction diagram		----
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]
show the reaction diagram		mechanism, (+)-biotinyl-5'-AMP is an intermediate in holotranscarboxylase synthesisPropionibacterium freudenreichii subsp. shermanii-1622

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
amination----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase (AMP-forming)-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
(+)-Biotin:methylmalonyl-CoA-pyruvate apocarboxyltransferase ligase (AMP)----
Biotin-apotranscarboxylase synthetase----
Biotin-methylmalonyl coenzyme A carboxyltransferase synthetase----
Biotin-transcarboxylase synthetase----
Biotin-[methylmalonyl-CoA-carboxyltransferase] ligase----
Biotin-[methylmalonyl-CoA-carboxyltransferase] synthetase----
biotin:apo[methylmalonyl-CoA:pyruvate carboxyltransferase] ligase (AMP-forming)----
Methylmalonyl coenzyme A holotranscarboxylase synthetase----
Synthetase, biotin-methylmalonyl coenzyme A carboxyltransferase----

CAS REGISTRY NUMBERCOMMENTARY
37318-66-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Propionibacterium freudenreichii subsp. shermanii-1619, 1620, 1621, 1622--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + biocytin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]?
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii--1619---
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii--1619-1619-
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii--1620---
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii-covalent attachment of biotin to the epsilon amino group to specific lysines of the enzyme, biotination of the apo-1.3SE subunit, MW 12000, the apo6SE, MW 144000, and the complete apotranscarboxylase, MW 1200000, occurs at approximately the same rates. Biotination occurs only on the 1.3SE subunit of the apotranscarboxylase1621---
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii-specific for (+)-biotin1622---
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]?
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii--1619---
CTP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]CMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii-23% of the activity relative to ATP1619---
GTP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]GMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii-18% of the activity relative to ATP1619---
ITP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]IMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii-5% of the activity relative to ATP1619---
UTP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]UMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii-4% of the activity relative to ATP1619---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]?
show the reaction diagram		Propionibacterium freudenreichii subsp. shermanii--1619--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Propionibacterium freudenreichii subsp. shermanii-affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0017 mM1620
Mg2+Propionibacterium freudenreichii subsp. shermanii-divalent metal ion required; Mg2+ or Mn2+1619
Mg2+Propionibacterium freudenreichii subsp. shermanii-affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+; divalent metal ion required; Km: 0.0019 mM1620
Mn2+Propionibacterium freudenreichii subsp. shermanii-divalent metal ion required, Mg2+ or Mn2+1619
Mn2+Propionibacterium freudenreichii subsp. shermanii-affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+; Km: 0.0015 mM1620
Ni2+Propionibacterium freudenreichii subsp. shermanii-affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0013 mM1620
Zn2+Propionibacterium freudenreichii subsp. shermanii-affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0003 mM1620

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(+)-Biotin methyl esterPropionibacterium freudenreichii subsp. shermanii--1619 2D-image
(+)-HomobiotinPropionibacterium freudenreichii subsp. shermanii--1619 2D-image
Co2+Propionibacterium freudenreichii subsp. shermanii-activates, inhibition at high concentrations1620 2D-image
Cu2+Propionibacterium freudenreichii subsp. shermanii--1620 2D-image
DL-O-HeterobiotinPropionibacterium freudenreichii subsp. shermanii--1619 2D-image
EDTAPropionibacterium freudenreichii subsp. shermanii--1619, 1620 2D-image
Hg2+Propionibacterium freudenreichii subsp. shermanii--1620 2D-image
Zn2+Propionibacterium freudenreichii subsp. shermanii-activates, inhibition at high concentrations1620 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Sulfhydryl compoundsPropionibacterium freudenreichii subsp. shermanii-activate1619 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00042-(+)-biotinPropionibacterium freudenreichii subsp. shermanii--1619, 1622 2D-image
0.0009-1.3S subunit of apotranscarboxylasePropionibacterium freudenreichii subsp. shermanii--1620-
0.038-ATPPropionibacterium freudenreichii subsp. shermanii--1620 2D-image
0.002-biotinPropionibacterium freudenreichii subsp. shermanii--1619 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.0124-Propionibacterium freudenreichii subsp. shermanii--1620
additional information-Propionibacterium freudenreichii subsp. shermanii--1619

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6-Propionibacterium freudenreichii subsp. shermanii--1620
7.2-Propionibacterium freudenreichii subsp. shermanii--1621
7.5-Propionibacterium freudenreichii subsp. shermanii--1619

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
68Propionibacterium freudenreichii subsp. shermanii-6.0: about 45% of maximal activity, 8.0: about 20% of maximal activity1619
6.47.4Propionibacterium freudenreichii subsp. shermanii-6.4: about 70% of maximal activity, 7.4: about 80% of maximal activity1621

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
37-Propionibacterium freudenreichii subsp. shermanii--1620

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2060Propionibacterium freudenreichii subsp. shermanii-about 30% of maximal activity at 20°C and 60°C1620

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
30000-Propionibacterium freudenreichii subsp. shermanii-gel filtration1620

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
monomerPropionibacterium freudenreichii subsp. shermanii-1 * 30000, SDS-PAGE1620

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
divalent metal is required for storage stability, Mg2+, Mn2+, Co2+, Zn2+, or Ni2+Propionibacterium freudenreichii subsp. shermanii-1620
loses activity by repeated freezing and thawingPropionibacterium freudenreichii subsp. shermanii-1620

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C, stable for 6 monthsPropionibacterium freudenreichii subsp. shermanii-1620

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Propionibacterium freudenreichii subsp. shermanii-1619, 1620, 1621

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
1619Lane, M.D.; Young, D.L.; Lynen, F.The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin. I. PURIFICATION OF THE APOENZYME AND SYNTHETASE; CHARACTERISTICS OF THE REACTIONJ. Biol. Chem.2392858-28641964Propionibacterium freudenreichii subsp. shermanii PubMed
1620Shenoy, B.C.; Wood, H.G.Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermaniiFASEB J.22396-24011988Propionibacterium freudenreichii subsp. shermanii PubMed
1621Wood, H.G.; Harmon, F.R.; Wuhr, B.; Hubner, K.; Lynen, F.Comparison of the biotination of apotranscarboxylase and its aposubunits. Is assembly essential for biotination ?J. Biol. Chem.2557397-74091980Propionibacterium freudenreichii subsp. shermanii PubMed
1622Lane, M.D.; Rominger, K.L.; Young, D.L.; Lynene, F.The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin. II. INVESTIGATION OF THE REACTION MECHANISM.J. Biol. Chem.2392865-28711964Propionibacterium freudenreichii subsp. shermanii PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 6.3.4.9)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)