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PMID:21625874
Citation |
Yu, ZL, Liu, J, Wang, FQ, Dai, M, Zhao, BH, He, JG and Zhang, H (2011) Cloning and characterization of a novel CoA-ligase gene from Penicillium chrysogenum. Folia Microbiol. (Praha) 56:246-52 |
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Abstract |
A novel phenylacetic acid (PAA)-induced CoA-ligase-encoding gene, designated as phlC, has been cloned from penicillin-producing fungus Penicillium chrysogenum. The open reading frame of phlC cDNA was 1671 bp and encoded a 556 amino acid residues protein with the consensus AMP binding site and a peroxisomal targeting signal 1 on its C terminus. The deduced amino acid sequence showed 37% and 38% identity with characterized P. chrysogenum Phl and PhlB protein, respectively. Functional recombinant PhlC protein was overexpressed in Escherichia coli. The purified recombinant enzyme was capable to convert PAA into its corresponding CoA ester with a specific activity of 129.5 ± 3.026 pmol/min per mg protein. Similar to Phl and PhlB, PhlC displayed broad substrate spectrum and showed higher activities to medium- and long-chain fatty acids. The catalytic properties of PhlC have been determined and compared to those of Phl and PhlB. |
Links |
PubMed Online version:10.1007/s12223-011-0044-y |
Keywords |
Acetyl Coenzyme A/biosynthesis; Amino Acid Sequence; Cloning, Molecular; Coenzyme A Ligases/chemistry; Coenzyme A Ligases/genetics; Coenzyme A Ligases/metabolism; Escherichia coli/genetics; Molecular Sequence Data; Penicillium chrysogenum/enzymology; Penicillium chrysogenum/genetics; Phenylacetates/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0047475: phenylacetate-CoA ligase activity |
ECO:0000315: |
F |
Figure 4b and 4c show the minimal activity due to lack of CoA substrate and without purified PhlC. However, when both substrate are present, there was a substantial increase in activity. Figure 2 shows that without PAA present, there are far fewer transcripts for PhlC since PAA and CoA are both needed in order for the protein to perform its ligase activity. |
complete | ||||
enables |
GO:0047475: phenylacetate-CoA ligase activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
Notes
See also
References
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