What question did this study set out to answer?

Identify and sequence the acvA gene in Aspergillus nidulans to characterize the molecular structure and domain organization of ACV synthetase.

July 1, 1991Journal of Biological ChemistryOpen Access

Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway

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Authors

AMAndrew MacCabeNortheastern University HLHenk van LiemptUniversity of St Andrews HPHarriet PalissaTechnische Universität Berlin

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Implication

Molecular genetic study uncovers the structure of the acvA gene in Aspergillus nidulans, revealing a modular nonribosomal mechanism for initial penicillin biosynthesis.

Key Points

Identify and sequence the acvA gene in Aspergillus nidulans to characterize the molecular structure and domain organization of ACV synthetase.
Matched a 15-amino acid sequence from a cyanogen bromide cleavage fragment of purified ACV synthetase against predicted genomic sequences to clone and sequence the complete acvA gene.
Estimated the native molecular weight using fast protein liquid chromatography and native gel electrophoresis, and evaluated glycosylation using concanavalin A affinity blotting.
Performed sequence alignments and comparative domain analyses against adenylate-forming enzymes and bacterial peptide synthetases.
The intronless acvA gene encodes a 3,770-amino acid glycoprotein with a molecular mass of 422,486 Da, transcribed in the opposite orientation to ipnA across an 872-nucleotide intergenic region.
The protein contains three homologous repeat units of approximately 585 residues matching adenylate-forming enzymes and nonribosomal peptide synthetases, alongside putative 4'-phosphopantetheine-attachment and thioesterase sites.
Conserved cysteine residues typical of the bacterial thiotemplate mechanism were absent from the ACV synthetase sequence despite high overall domain homology.

Cite This Study

MacCabe et al. (1991) studied this question.

synapsesocial.com/papers/6a83334288eff2bd7befeeda https://doi.org/10.1016/s0021-9258(18)98948-9

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Implication

Molecular genetic study uncovers the structure of the acvA gene in Aspergillus nidulans, revealing a modular nonribosomal mechanism for initial penicillin biosynthesis.

Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway

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Key Points

Cite This Study

Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway

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Key Points

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