Use of long-chain fatty acid-CoA ligase (AMP-forming) from Pseudomonas fragi for the 'in vitro' synthesis of natural penicillins.
Five different naturally occurring penicillins containing as side chains hexanoic, trans-3-hexenoic, heptanoic, octanoic or trans-3-octenoic acids have been synthesized 'in vitro' by coupling long-chain fatty acid-CoA ligase (AMP-forming) (EC 6.2.1.3) from Pseudomonas fragi (LFCoA-L) with acyl-CoA: 6-aminopenicillanic acid acyltransferase (AT) from Penicillium chrysogenum. The quantity of penicillin produced was directly related with the carbon length of the side chain precursor tested, being maximal with octanoic acid. Fatty acids with a lower length than C5 were not recognized as substrates and nor were certain aromatic molecules.
Fernández-Valverde
M
M
Departamento de Bioquímica y Biología Molecular, Facultad de Veterinaria, Universidad de León, Spain.
Reglero
A
A
Luengo
J M
JM
D000214:Acyl Coenzyme A / Q000378:metabolism; D000217:Acyltransferases / Q000378:metabolism; D003066:Coenzyme A Ligases / Q000378:metabolism*; D005227:Fatty Acids; D010397:Penicillanic Acid / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000096:biosynthesis*; D011549:Pseudomonas / Q000378:metabolism*; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D000214:Acyl Coenzyme A; D005227:Fatty Acids; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D010397:Penicillanic Acid; D000217:Acyltransferases; C018756:acyl-CoA-6-aminopenicillanic acid acyltransferase; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase