Synergistic Action of an X-Prolyl Dipeptidyl Aminopeptidase and a Non-Specific Aminopeptidase in Protein Hydrolysis

Byun, Tony; Kofod, Lene V.; Blinkovsky, Alexander M.

doi:10.1021/jf001091m

Cited by 46 publications

(25 citation statements)

References 11 publications

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“…Protein digestion into amino acids has been thoroughly investigated in micro-organisms used in the food fermentation industry. Bacteria of the genus Lactobacillus (O'Cuinn et al, 1999) and fungi of the genus Aspergillus (Byun et al, 2001;Doumas et al, 1998) secrete endo-and exoproteases, which cooperate efficiently in protein digestion. The main function of the former is to produce a large number of free ends on which the latter may act.…”

Section: Discussionmentioning

confidence: 99%

Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum

et al. 2005

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The nature of secreted aminopeptidases in Trichophyton rubrum was investigated by using a reverse genetic approach. T. rubrum genomic and cDNA libraries were screened with Aspergillus spp. and Saccharomyces cerevisiae aminopeptidase genes as the probes. Two leucine aminopeptidases, ruLap1 and ruLap2, and two dipeptidyl-peptidases, ruDppIV and ruDppV, were characterized and compared to orthologues secreted by Aspergillus fumigatus using a recombinant protein from Pichia pastoris. RuLap1 is a 33 kDa nonglycosylated protein, while ruLap2 is a 58-65 kDa glycoprotein. The hydrolytic activity of ruLap1, ruLap2 and A. fumigatus orthologues showed various preferences for different aminoacyl-7-amido-4-methylcoumarin substrates, and various sensitivities to inhibitors and cations. ruDppIV and ruDppV showed similar activities to A. fumigatus orthologues. In addition to endopeptidases, the four aminopeptidases ruLap1, ruLap2, ruDppIV and ruDppV were produced by T. rubrum in a medium containing keratin as the sole nitrogen source. Synergism between endo-and exopeptidases is likely to be essential for dermatophyte virulence, since these fungi grow only in keratinized tissues.

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Section: Discussionmentioning

confidence: 99%

Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum

et al. 2005

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“…The 73 KD protein was identical to Xaa-Pro aminopeptidase, matching AO090701000720 and AoEST01711 without a predicted N-terminal signal sequence, was responsible for the release of all N-terminal amino acid adjacent to a proline residue and the synergistic action of a Xaa-Pro aminopeptidase and a non-specific aminopeptidase in protein hydrolysis. 14,15) Glutaminase is thought to play an important role in producing the flavor of soy sauce by catalyzing L-glutamine transformation to L-glutamate. AO090020000289, containing the predicted signal pep- a, Band no.…”

Section: 4)mentioning

confidence: 99%

Analysis of Extracellular Proteins ofAspergillus oryzaeGrown on Soy Sauce Koji

Yan-chang¹,

Pan²,

Lin³

2009

Bioscience, Biotechnology, and Biochemistry

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“…Synergism of non-specific amino peptidases (Lap at neutral pH, Seds at low pH) and prolyl peptidases (DppIV or AfuS28 at neutral pH, AfuS28 at low pH) allows sequential degradation of large peptides previously generated by endoproteolysis into amino acids, and di-and tripeptides (Byun et al, 2001;Sriranganadane et al, 2010). Large peptide cleavage by further exoproteolytic activity is also essential for fungi using protein as sole nitrogen and carbon source as only amino acids and short peptides can be assimilated by transporters.…”

Section: Discussionmentioning

confidence: 99%

Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium

et al. 2011

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In an acidic protein medium Aspergillus fumigatus secretes an aspartic endoprotease (Pep) as well as tripeptidyl-peptidases, a prolyl-peptidase and carboxypeptidases. In addition, LC-MS/MS revealed a novel glutamic protease, AfuGprA, homologous to Aspergillus niger aspergillopepsin II. The importance of AfuGprA in protein digestion was evaluated by deletion of its encoding gene in A. fumigatus wild-type D141 and in a pepΔ mutant. Either A. fumigatus Pep or AfuGprA was shown to be necessary for fungal growth in protein medium at low pH. Exoproteolytic activity is therefore not sufficient for complete protein hydrolysis and fungal growth in a medium containing proteins as the sole nitrogen source. Pep and AfuGprA constitute a pair of endoproteases active at low pH, in analogy to A. fumigatus alkaline protease (Alp) and metalloprotease I (Mep), where at least one of these enzymes is necessary for fungal growth in protein medium at neutral pH. Heterologous expression of AfuGprA in Pichia pastoris showed that the enzyme is synthesized as a preproprotein and that the propeptide is removed through an autoproteolytic reaction at low pH to generate the mature protease. In contrast to A. niger aspergillopepsin II, AfuGprA is a single-chain protein and is structurally more similar to G1 proteases characterized in other non-Aspergillus fungi.

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Synergistic Action of an X-Prolyl Dipeptidyl Aminopeptidase and a Non-Specific Aminopeptidase in Protein Hydrolysis

Cited by 46 publications

References 11 publications

Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum

Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum

Analysis of Extracellular Proteins ofAspergillus oryzaeGrown on Soy Sauce Koji

Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium

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