2001
DOI: 10.1074/jbc.m106353200
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Abstract: Biotin carboxyl carrier protein (BCCP) is the small biotinylated subunit of Escherichia coli acetyl-CoA carboxylase (ACC), the enzyme that catalyzes the first committed step of fatty acid synthesis. Similar proteins are found in other bacteria and in chloroplasts. E. coli BCCP is a member of a large family of protein domains modified by covalent attachment of biotin to a specific lysine residue. However, the BCCP biotinyl domain differs from many of these proteins in that an eight-amino acid residue insertion … Show more

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Cited by 61 publications
(50 citation statements)
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“…In the absence of expression of a functional plasmid-encoded BCCP gene, strain CY1336 fails to grow, whereas expression of a functional protein permits growth (hence giving genetic complementation of the host accB mutation). At 37°C, growth was found to require about 8% of the normal level of BCCP (28). Strain CY1336 expressing the wild type gene grows well at 37°C and appreciably more slowly at 42°C.…”
Section: Resultsmentioning
confidence: 99%
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“…In the absence of expression of a functional plasmid-encoded BCCP gene, strain CY1336 fails to grow, whereas expression of a functional protein permits growth (hence giving genetic complementation of the host accB mutation). At 37°C, growth was found to require about 8% of the normal level of BCCP (28). Strain CY1336 expressing the wild type gene grows well at 37°C and appreciably more slowly at 42°C.…”
Section: Resultsmentioning
confidence: 99%
“…Finally, none of the BCCP residues upstream of residue 81 show any structure-based alignment with the other biotinyl domain of known structure, the P. shermanii 1.3 S trancarboxylase subunit (28), indicating that these residues do not play a role in biotin domain structure.…”
Section: Resultsmentioning
confidence: 99%
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“…Mössbauer spectra of whole cell preparations of E. coli expressing recombinant BioB indicate that <35% of the enzyme contains a [4Fe-4S] 2+ cluster, probably due to the air-sensitivity of this cluster [18,19]. Since the biotin requirements of bacteria are very low, on the order of 100-1000 molecules per cell [20], it has been suggested that BioB may be a stoichiometric reactant that is degraded after a single turnover. However, Choi-Rhee and Cronan have recently used a combination of 35 S-methionine protein labeling and Western blots to analyze the production of biotin from BioB under conditions that suppress new protein synthesis [21].…”
Section: Introductionmentioning
confidence: 99%