Abstract:
:Coenzyme A ligases play an important role in metabolism by catalyzing the activation of carboxylic acids. In this study we describe the synthesis of aminoacyl-coenzyme As (CoAs) catalyzed by a CoA ligase from Penicillium chrysogenum. The enzyme accepted medium-chain length fatty acids as the best substrates, but the proteinogenic amino acids L-phenylalanine and L-tyrosine, as well as the non-proteinogenic amino acids D-phenylalanine, D-tyrosine and (R)- and (S)-β-phenylalanine were also accepted. Of these amino acids, the highest activity was found for (R)-β-phenylalanine, forming (R)-β-phenylalanyl-CoA. Homology modeling suggested that alanine 312 is part of the active site cavity, and mutagenesis (A312G) yielded a variant that has an enhanced catalytic efficiency with β-phenylalanines and D-α-phenylalanine.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Koetsier MJ,Jekel PA,Wijma HJ,Bovenberg RA,Janssen DBdoi
10.1016/j.febslet.2011.02.018subject
Has Abstractpub_date
2011-03-23 00:00:00pages
893-8issue
6eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00119-0journal_volume
585pub_type
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