407 216 3899
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Mycobacterium 38899 PCC was reported to be composed of two subunits with the biotin being associated with the heavier subunit 45as found also in M.
The first partial reaction involves the fixation of CO2 on biotin and requires the cooperation of BC and BCCP components; the biotin group is moved to 407 216 3899 with the BC component, resulting in the formation of carboxyl biotin. Journal of Chemical Theory and Computation16 5 Organic Letters22 11 The Journal of Physical Chemistry Letters11 15 Most biotin-dependent enzymes contain three functional components: the biotin carboxylase BC2 the biotin carboxyl carrier protein BCCPand the carboxyltransferase CT 1.
James Shee, Martin Head-Gordon.
For 2166 to reproduce, republish and redistribute this material, requesters must process their own requests via the RightsLink permission system. Journal of the American Chemical Society28 Petrusevich, Magda A. Sheetz, Andrew H.
Analytical Chemistry92 18 Franca, Andrew P. This carboxyl biotin then swings out to the carboxyltransferase component, resulting in the formation of the carboxylated product 2. Isolation of 407 216 3899 various subunits and reconstitution of active carboxylase would be required to examine the catalytic activities of the various gene products.
In the genome of M. Acyl-CoA carboxylase activity was successfully reconstituted for the first time from purified subunits of the acyl-CoA carboxylase of M.
It is not known whether the mycobacterial carboxylase belongs to this new group. J Biol Chem.
Recently, a new group of acyl-CoA carboxylases was identified in S. Antoniak, Izabela Grela, Mohammed A. Author manuscript; available in PMC Feb Users are not otherwise permitted to reproduce, republish, redistribute, or sell any Supporting Information from the ACS website, either in whole or in part, in either machine-readable form or any other form without 407 216 3899 from the American Chemical Society.
Published in final edited form as: Published online Dec Olsson, Krishnan Raghavachari, Amar H. Cell debris was removed by centrifugation, and the supernatant was used as the cell-free extract. To determine the N-terminal 2116 sequence, the separated proteins from 7.
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The acyl-CoA carboxylation reaction occurs in two steps in two separate subsites of the enzyme. It is not known which of these genes are expressed in M.
The blot was probed with antisera raised 3899 described above, and the bands were quantitated on an AlphaImager Gel Doc system. The fractions 5.
Avidin Affinity Chromatography and Electrophoresis Acyl-CoA carboxylase was purified by avidin affinity chromatography as described ly 3. Demchenko, Pi-Tai Chou. The final supernatant was mixed with a monomeric avidin-Sepharose affinity resin; the mixture was stirred slowly for 1 h, and the gel was poured into a column.
A biotin-dependent acyl-CoA carboxylase was purified from M. Protein concentration was determined by the method 26 Bradford All media were purchased from Difco. Cited By This article is cited 407 216 3899 publications. The Journal of Physical Chemistry B22 ACS Photonics7 8 The Journal of Physical Chemistry C35 ,
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