Kinamycin acetyltransferase I from Streptomyces murayamaensis, an apparently large, membrane-associated enzyme.
Identification and initial characterization of an apparently large, membrane-associated multifunctional enzyme, kinamycin acetyltransferase I (KAT I), is described. KAT I activity was enriched 29-fold over the level in cell-free extracts of Streptomyces murayamaensis. Two acetyltransferase activities catalyzing acetyl coenzyme A dependent conversion of kinamycin F and E to kinamycin E and D, respectively, were inseparable in the course of the partial purification. Partial purification involved separation of KAT I from cytosolic proteins by differential ultracentrifugation, solubilization with 0.5% CHAPS zwitterionic detergent followed by ultracentrifugation, and Sephacryl S400 gel filtration chromatography of the resulting supernatant.
Gould
S J
SJ
Department of Chemistry, Oregon State University, Corvallis 97331-4003, USA.
O'Hare
T
T
Seaton
P
P
Soodsma
J
J
Tang
Z
Z
D000123:Acetyltransferases / Q000378:metabolism*; D002227:Carbazoles / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011809:Quinones / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D000095602:Angucyclines and Angucyclinones
D000123:Acetyltransferases; D002227:Carbazoles; D011809:Quinones; C059020:kinamycin E; D000095602:Angucyclines and Angucyclinones; C088442:kinamycin D; C059021:kinamycin F; C103393:kinamycin acetyltransferase I