2008
DOI: 10.1111/j.1365-2672.2008.03889.x
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Efficient production and partial characterization of aspartyl aminopeptidase fromAspergillus oryzae

Abstract: Aims:  Aspartyl aminopeptidase (DAP) has a high degree of substrate specificity, degrading only amino‐terminal acidic amino acids from peptides. Therefore, attention is focused here on the efficient production of this enzyme by a recombinant Aspergillus oryzae and characterization of its biochemical properties. Methods and Results:  The gene encoding DAP was overexpressed under a taka‐amylase gene promoter, with His‐tag linker in A. oryzae, during cultivation in a Co2+‐containing medium. The enzyme was extract… Show more

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Cited by 28 publications
(20 citation statements)
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“…Immunoblot analysis indicated the 120-kDa band contained His 6 -DAP1 and is likely to represent a DAP dimer (data not shown). DAP dimers have been detected for the Aspergillus DAP, Plasmodium M18APP, and mammalian DNPEP [17, 19, 55]. Dimers are known to be an assembly intermediate for the human and Plasmodium dodecamer [17, 19].…”
Section: Resultsmentioning
confidence: 99%
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“…Immunoblot analysis indicated the 120-kDa band contained His 6 -DAP1 and is likely to represent a DAP dimer (data not shown). DAP dimers have been detected for the Aspergillus DAP, Plasmodium M18APP, and mammalian DNPEP [17, 19, 55]. Dimers are known to be an assembly intermediate for the human and Plasmodium dodecamer [17, 19].…”
Section: Resultsmentioning
confidence: 99%
“…oryzea ), Plasmodium and mouse [10, 16, 18, 67]. In contrast, other DAPs were preferentially inhibited by one chelator but not the other [12, 55]. These different responses to chelators may reflect the redox state of residues within the catalytic site.…”
Section: Discussionmentioning
confidence: 99%
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“…In particular, the behavior of the enzyme showed similarity to those of the aspartyl aminopeptidases from yeast and Aspergillus oryzae in its enzymatic characterization. [20][21][22] Aspartyl aminopeptidase has been reported to be present in mammals, yeast, and filamentous fungi, but has not previously been purified from plants. [20][21][22] To confirm that the enzyme was aspartyl aminopeptidase, we intend to determine the amino acid sequence of the enzyme and to compare them of the known aspartyl aminopeptidases.…”
Section: Substrate Specificitymentioning
confidence: 99%
“…15) Aminopeptidase, which liberates glutamic acid or aspartic acid from the N-terminus of peptide, is called glutamyl aminopeptidase [16][17][18] or aspartyl aminopeptidase. 19,20) These enzymes have been reported to be present in mammals, yeast, and filamentous fungi, [20][21][22] but have not been purified from plants.…”
mentioning
confidence: 99%