Literature summary for 6.3.4.9 extracted from

Wood, 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 ? (1980), J. Biol. Chem., 255, 7397-7409.

Search for more literature for 6.3.4.9

Organism

Organism	UniProt	Comment	Textmining
Propionibacterium freudenreichii subsp. shermanii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]	covalent attachment of biotin to the epsilon amino group to specific lysines of the enzyme	Propionibacterium freudenreichii subsp. shermanii	AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]	-	?
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]	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 apotranscarboxylase	Propionibacterium freudenreichii subsp. shermanii	AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]	-	?

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	-	Propionibacterium freudenreichii subsp. shermanii

pH Range

pH Minimum	pH Maximum	Comment	Organism
6.4	7.4	6.4: about 70% of maximal activity, 7.4: about 80% of maximal activity	Propionibacterium freudenreichii subsp. shermanii

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Release 2023.1 (January 2023)