About: Heterologous expression and characterization of CpI, OcpA, and novel serine-type carboxypeptidase OcpB from Aspergillus oryzae

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About: Heterologous expression and characterization of CpI, OcpA, and novel serine-type carboxypeptidase OcpB from Aspergillus oryzae Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Heterologous expression and characterization of CpI, OcpA, and novel serine-type carboxypeptidase OcpB from Aspergillus oryzae
Creator	Ishida, Hiroki Koide, Yoshinao Morita, Hiroto Okamoto, Ayako Takeuchi, Michio Yamagata, Yohei Kusumoto, Ken-Ichi
topic	covid:77e0e1f217c31919a3102a3abd427bebd8b5c354#this
source	PMC
abstract	In the genome of Aspergillus oryzae, 12 genes have been predicted to encode serine-type carboxypeptidases. However, the carboxypeptidase activities of the proteins encoded by these genes have not yet been confirmed experimentally. In this study, we have constructed three of these 12 genes overexpressing strains using Aspergillus nidulans and characterized their overproduced recombinant proteins. Of these three genes, one was previously named cpI; the other two have not been reported yet, and hence, we named them ocpA and ocpB. The recombinant proteins released amino acid residues from the C terminus of peptides, and the activity of the enzymes was inhibited by phenylmethylsulfonyl fluoride, indicating the enzymes to be serine-type carboxypeptidases. Recombinant OcpA, OcpB, and CpI were stable at 45°C, 55°C, and 55°C, respectively, at a low pH. The enzymatic properties of recombinant OcpB were different from those of any reported serine-type carboxypeptidase. On the other hand, recombinant OcpA had similar enzymatic properties to A. oryzae carboxypeptidases O1 and O2. The DNA and N-terminal amino acid sequences of carboxypeptidases O1 and O2 from A. oryzae IAM2640 were similar to those of OcpA. Result of transcriptional analysis of ocpA, ocpB, and cpI suggest differences in transcriptional regulation between these genes.
has issue date	2009-06-26(xsd:dateTime)
bibo:doi	10.1007/s00253-009-2087-4
bibo:pmid	19557408
has license	no-cc
sha1sum (hex)	77e0e1f217c31919a3102a3abd427bebd8b5c354
schema:url	https://doi.org/10.1007/s00253-009-2087-4
resource representing a document's title	Heterologous expression and characterization of CpI, OcpA, and novel serine-type carboxypeptidase OcpB from Aspergillus oryzae
has PubMed Central identifier	PMC2773364
has PubMed identifier	19557408
schema:publication	Appl Microbiol Biotechnol
resource representing a document's body	covid:77e0e1f217c31919a3102a3abd427bebd8b5c354#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/77e0e1f217c31919a3102a3abd427bebd8b5c354
is schema:about of	named entity 'carboxypeptidase' named entity 'confirmed' named entity 'activity' named entity 'sequences' named entity 'C terminus' named entity 'recombinant proteins' named entity 'carboxypeptidase' named entity 'carboxypeptidase' named entity 'Heterologous' named entity 'CARBOXYPEPTIDASE' named entity 'STUDY' covid:arg/77e0e1f217c31919a3102a3abd427bebd8b5c354 named entity 'genes' named entity 'recombinant' named entity 'recombinant' named entity 'enzymatic' named entity 'genes' named entity 'indicating' named entity 'Recombinant' named entity 'serine' named entity 'transcriptional' named entity 'carboxypeptidases' named entity 'peptides' named entity 'A. oryzae' named entity 'serine' named entity 'carboxypeptidases' named entity '30°C' named entity 'pH 3' named entity 'carboxypeptidase' named entity 'PCR' named entity 'carboxypeptidases' named entity 'Gly' named entity 'A50' named entity 'His-tag' named entity 'acetate' named entity 'amino acid sequences' named entity 'recombinants' named entity 'sephadex' named entity 'transcription' named entity 'serine' named entity 'substrate' named entity 'electrophoresis' named entity 'fungus' named entity 'S 1' named entity 'Hilden' named entity 'angiotensin' named entity 'α-cyano-4-hydroxycinnamic acid' named entity 'substrate specificity' named entity 'substrate specificities' named entity 'w/v' named entity 'Tyr' named entity 'protein' named entity 'glucose' named entity 'carboxypeptidases' named entity 'A. oryzae' named entity 'overexpressing' named entity 'Aspergillus' named entity 'start codon' named entity 'carboxypeptidases' named entity '30°C' named entity 'PCR amplification' named entity 'Tyr' named entity 'motif' named entity 'eluted' named entity 'protease inhibitors' named entity 'heterologous expression' named entity 'pH 3' named entity 'genomic DNA' named entity 'amino acid sequences' named entity 'carboxypeptidase' named entity 'Cys' named entity 'nitrogen' named entity 'recombinants'

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