Synthesis of Acetyl Coenzyme A Holocarboxylase in Vitro by a Cytosolic Preparation from Chicken Liver

Murthy, Padala Narasimha; Mistry, S. P.

doi:10.3181/00379727-147-38292

Cited by 3 publications

(2 citation statements)

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“…Biotinylation of BCCP is also thought to be possible both before and after assembly into acetyl-CoA carboxylase. Biotinylation studies on E. coli, chicken and human apoacetyl-CoA carboxylases [25][26][27], and on fusion proteins containing biotinyl domains [23,24], support this conclusion. This suggests that the biocytin 3 hairpin, notably Lys122, must be near the surface to facilitate biotinylation by BirA as well as the intersubunit translocation of the biotinyl moiety.…”

Section: Functional Interactions Of Bccpmentioning

confidence: 90%

“…Thus, bacterial holocarboxylase synthetase can biotinylate rat apocarboxylases [21,22]. Only the biotinyl domain of apocarboxylase is necessary for biotinylation [23,24], although synthetases can biotinylate intact apocarboxylases [25][26][27]. Thus, we expect that an analysis of biotinylation of BCCPsc by the E. coli holocarboxylase synthetase (BirA) [25,28], the structure of which is known [29], will enhance our understanding of biotinylation in man.…”

Section: Introductionmentioning

confidence: 99%

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Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing

1995

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This first crystal structure of a biotinyl domain helps to unravel the central role of such domains in reactions catalyzed by biotin-dependent carboxylases. The hammerhead structure observed twice in BCCPsc may be regarded as the basic structural motif of biotinyl and lipoyl domains of a superfamily of enzymes. The new MAD phasing techniques developed in the course of determining this structure enhance the power of the MAD method.

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