Extracellular production and characterization of Streptomyces X-prolyl dipeptidyl aminopeptidase. 2011

Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
Okayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS), Okayama, Kibichuo-cho, Kaga-gun, Japan. hatanaka@bio-ribs.com

X-prolyl dipeptidyl aminopeptidases (X-PDAPs) are useful in various food industries. In this study, we performed sequence-based screening to obtain a stable X-PDAP enzyme from thermophilic Streptomyces strains. We found three genes that encoded X-PDAP from Streptomyces thermoluteus subsp. fuscus NBRC 14270 (14270 X-PDAP), Streptomyces thermocyaneoviolaceus NBRC 14271 (14271 X-PDAP), and Streptomyces thermocoerulescens NBRC 14273, which were subsequently cloned and sequenced. The deduced amino acid sequences of these genes showed high similarity, with ~80% identity with each other. The isolated X-PDAPs and an X-PDAP from Streptomyces coelicolor were expressed in Streptomyces lividans using a hyperexpression vector: pTONA5a. Among these genes, only 14270 and 14271 X-PDAPs caused overexpression and extracellular production without artificial signal peptides. We also characterized the biochemical properties of purified 14271 X-PDAP. In addition, we found that, in peptide synthesis via an aminolysis reaction, this enzyme recognized D-amino acid derivatives as acyl acceptors, similar to L-amino acid derivatives.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D004152 Dipeptidyl-Peptidases and Tripeptidyl-Peptidases A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain. Dipeptidyl Peptidase,Dipeptidyl Peptidases,Dipeptidylpeptide Hydrolase,Tripeptidyl-Peptidase,Dipeptidylpeptide Hydrolases,Tripeptidyl-Peptidases,Dipeptidyl Peptidases and Tripeptidyl Peptidases,Hydrolase, Dipeptidylpeptide,Peptidase, Dipeptidyl,Tripeptidyl Peptidase,Tripeptidyl Peptidases,Tripeptidyl-Peptidases and Dipeptidyl-Peptidases
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D013302 Streptomyces A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures
D021382 Protein Sorting Signals Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments. Leader Signal Peptides,Leader Peptide,Leader Sequences, Peptide,Peptide Leader Sequences,Peptide Signal Sequences,Signal Peptide,Signal Peptides,Signal Sequence, Peptide,Signal Sequences,Signal Sequences, Peptide,Leader Peptides,Leader Sequence, Peptide,Leader Signal Peptide,Peptide Leader Sequence,Peptide Signal Sequence,Peptide, Leader,Peptide, Leader Signal,Peptide, Signal,Peptides, Leader,Peptides, Leader Signal,Peptides, Signal,Protein Sorting Signal,Sequence, Peptide Leader,Sequence, Peptide Signal,Sequence, Signal,Sequences, Peptide Leader,Sequences, Peptide Signal,Sequences, Signal,Signal Peptide, Leader,Signal Peptides, Leader,Signal Sequence,Signal, Protein Sorting,Signals, Protein Sorting,Sorting Signal, Protein,Sorting Signals, Protein

Related Publications

Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
January 1980, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
August 1976, Analytical biochemistry,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
April 1987, Journal of dairy science,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
January 1992, International journal of food microbiology,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
November 1983, Journal of general microbiology,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
July 1993, Applied and environmental microbiology,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
December 1995, Microbiology (Reading, England),
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
October 1979, Experientia,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
April 2001, Journal of agricultural and food chemistry,
Tadashi Hatanaka, and Akihiro Yamasato, and Jiro Arima, and Hirokazu Usuki, and Yukihiro Yamamoto, and Yuya Kumagai
January 1995, Analytical biochemistry,
Copied contents to your clipboard!