Publication | Closed Access
Analysis of type II polyketide beta-ketoacyl synthase specificity in Streptomyces coelicolor A3(2) by trans complementation of actinorhodin synthase mutants
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Citations
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References
1994
Year
EngineeringSpore Pigment KssOrf2-encoded Ks ComponentMolecular BiologyTrans ComplementationType IiBiosynthesisNatural Product BiosynthesisStructure-function Enzyme KineticsOrf1-encoded KsActinorhodin Synthase MutantsBiotransformationBiochemistryMolecular MicrobiologyProtein BiosynthesisBiologyNatural SciencesBiotechnologyMicrobiology
Complementation of defined actinorhodin beta-ketoacyl synthase (KS) mutants by various other KS genes suggested that the ORF1-encoded KS may be relatively generalized in function, whereas the ORF2-encoded KS component may provide specificity in polyketide chain construction. Evidence for differential temporal-spatial expression of the actinorhodin and spore pigment KSs in Streptomyces coelicolor was obtained.
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