Open AccessTRANSCARBOXYLASE, VIII. ISOLATION AND PROPERTIES OF A BIOTIN-CARBOXYL CARRIER PROTEIN
Author(s) -
Brenda I. Gerwin,
Bertil Jacobson,
Harland G. Wood
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.64.4.1315
Subject(s) - biotin , propionibacterium , chemistry , cystine , protein subunit , mole , alanine , enzyme , biochemistry , residue (chemistry) , amino acid , biology , cysteine , genetics , bacteria , gene
Methylmalonyl CoA-oxalacetate transcarboxylase (EC 2. 1. 3. 1) fromPropionibacterium shermanii is a biotin enzyme of 670,000 molecular weight containing 6 moles of biotin per mole of enzyme. The active enzyme dissociates spontaneously at low ionic strength and alkaline pH to a mixture of inactive subunits. One type of subunit contains all the biotin of the original molecule. The biotin unit has anS20,w = 1.3S and a molecular weight of approximately 12,000. It contains 1 mole of biotin and 1 half-cystine per mole. Qualitative dansyl techniques indicate that alanine is the amino terminal residue of the biotin subunit.