2026-09-21T19:45:43Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/86735 2023-07-11 col_2142_5131 col_2142_16338 com_2142_5130 com_2142_16337 com_2142_14793 com_2142_8903

Cronan, John E., Jr Davis, Mark Stephen 2015-09-28T15:17:44Z 2015-09-28T15:17:44Z 10000-01-01 1998 1998 Preliminary functional assignments for the two subunits in the carboxyltransferase complex have been given. The alpha subunit (AccA) appears to have a structural role in the total ACC complex while the beta subunit (AccD) could contain the carboxyltransferase active site. The above conclusions are based on enzymatic deactivational studies with extracts only overproducing AccBCD with and without PEG (14%) compared to extracts with all four subunits overproduced (AccABCD) for the assignment of the AccA function. Extracts only overproducing AccD contained higher carboxyltransferase activity leading one to conclude the active site for the complex is contained in the AccD subunit. Made available in DSpace on 2015-09-28T15:17:44Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9912216.pdf: 4873900 bytes, checksum: 81f609d6366f04508b770a89fea22f67 (MD5) Previous issue date: 1998 Embargo set by: Seth Robbins for item 88016 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 134 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998. http://hdl.handle.net/2142/86735 (MiAaPQ)AAI9912216 eng Biology, Molecular Studies of Acetyl-Coa Carboxylase From Escherichia Coli text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.