scholarly journals A Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptidesin Vitro

2018 ◽  
Vol 13 (9) ◽  
pp. 2513-2521 ◽  
Author(s):  
Janice H. Xu ◽  
Zhenze Jiang ◽  
Angelo Solania ◽  
Sandip Chatterjee ◽  
Brian Suzuki ◽  
...  
Keyword(s):  
Dipeptidyl Aminopeptidase

scholarly journals Purification of Dipeptidyl Aminopeptidase II (Dipeptidyl Arylamidase II) of the Anterior Pituitary Gland

1968 ◽  
Vol 243 (15) ◽  
pp. 4143-4150 ◽  
Author(s):  
J K McDonald ◽  
F H Leibach ◽  
R E Grindeland ◽  
S Ellis
Keyword(s):  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Anterior Pituitary Gland ◽  
Dipeptidyl Aminopeptidase

Diprotin, an inhibitor of dipeptidyl aminopeptidase IV(EC 3.4.14.5) produces naloxone — reversible analgesia in rats

Life Sciences ◽  
1998 ◽  
Vol 64 (2) ◽  
pp. 145-152 ◽  
Author(s):  
András Z. Rónai ◽  
Julianna Timár ◽  
Éva Makó ◽  
Franciska Erdóo ◽  
Zsuzsanna Gyarmati ◽  
...  
Keyword(s):  
Dipeptidyl Aminopeptidase

scholarly journals A Dipeptidyl Aminopeptidase–like Protein Remodels Gating Charge Dynamics in Kv4.2 Channels

2006 ◽  
Vol 128 (6) ◽  
pp. 745-753 ◽  
Author(s):  
Kevin Dougherty ◽  
Manuel Covarrubias
Keyword(s):  
Membrane Potentials ◽  
Charge Movement ◽  
Transmembrane Segment ◽  
Gating Currents ◽  
Voltage Sensing ◽  
Charge Voltage ◽  
Charge Dynamics ◽  
Gating Charge ◽  
Kv4 Channels ◽  
Dipeptidyl Aminopeptidase

Dipeptidyl aminopeptidase–like proteins (DPLPs) interact with Kv4 channels and thereby induce a profound remodeling of activation and inactivation gating. DPLPs are constitutive components of the neuronal Kv4 channel complex, and recent observations have suggested the critical functional role of the single transmembrane segment of these proteins (Zagha, E., A. Ozaita, S.Y. Chang, M.S. Nadal, U. Lin, M.J. Saganich, T. McCormack, K.O. Akinsanya, S.Y. Qi, and B. Rudy. 2005. J. Biol. Chem. 280:18853–18861). However, the underlying mechanism of action is unknown. We hypothesized that a unique interaction between the Kv4.2 channel and a DPLP found in brain (DPPX-S) may remodel the channel's voltage-sensing domain. To test this hypothesis, we implemented a robust experimental system to measure Kv4.2 gating currents and study gating charge dynamics in the absence and presence of DPPX-S. The results demonstrated that coexpression of Kv4.2 and DPPX-S causes a −26 mV parallel shift in the gating charge-voltage (Q-V) relationship. This shift is associated with faster outward movements of the gating charge over a broad range of relevant membrane potentials and accelerated gating charge return upon repolarization. In sharp contrast, DPPX-S had no effect on gating charge movements of the Shaker B Kv channel. We propose that DPPX-S destabilizes resting and intermediate states in the voltage-dependent activation pathway, which promotes the outward gating charge movement. The remodeling of gating charge dynamics may involve specific protein–protein interactions of the DPPX-S's transmembrane segment with the voltage-sensing and pore domains of the Kv4.2 channel. This mechanism may determine the characteristic fast operation of neuronal Kv4 channels in the subthreshold range of membrane potentials.

scholarly journals Transcriptome and Proteome Expression Analysis of the Metabolism of Amino Acids by the FungusAspergillus oryzaein Fermented Soy Sauce

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Guozhong Zhao ◽  
Yunping Yao ◽  
Chunling Wang ◽  
Fengwei Tian ◽  
Xiaoming Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Gel Electrophoresis ◽  
Metabolic Pathways ◽  
Soy Sauce ◽  
Flavor Compounds ◽  
Acid Hydrolases ◽  
Conserved Genes ◽  
2D Gel ◽  
Dipeptidyl Aminopeptidase ◽  
Proteome Expression

Amino acids comprise the majority of the flavor compounds in soy sauce. A portion of these amino acids are formed from the biosynthesis and metabolism of the fungusAspergillus oryzae; however, the metabolic pathways leading to the formation of these amino acids inA. oryzaeremain largely unknown. We sequenced the transcriptomes ofA. oryzae100-8 andA. oryzae3.042 under similar soy sauce fermentation conditions. 2D gel electrophoresis was also used to find some differences in protein expression. We found that many amino acid hydrolases (endopeptidases, aminopeptidases, and X-pro-dipeptidyl aminopeptidase) were expressed at much higher levels (mostly greater than double) inA. oryzae100-8 than inA. oryzae3.042. Our results indicated that glutamate dehydrogenase may activate the metabolism of amino acids. We also found that the expression levels of some genes changed simultaneously in the metabolic pathways of tyrosine and leucine and that these conserved genes may modulate the function of the metabolic pathway. Such variation in the metabolic pathways of amino acids is important as it can significantly alter the flavor of fermented soy sauce.

scholarly journals Whole genome sequencing reveals the genomic diversity, taxonomic classification, and evolutionary relationships of the genus Nocardia

2021 ◽  
Vol 15 (8) ◽  
pp. e0009665
Author(s):  
Shuai Xu ◽  
Zhenpeng Li ◽  
Yuanming Huang ◽  
Lichao Han ◽  
Yanlin Che ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Phylogenetic Trees ◽  
Gene Families ◽  
Single Copy ◽  
Taxonomic Classification ◽  
Genomic Diversity ◽  
Evolutionary Relationships ◽  
Taxonomic Structure ◽  
Pan Genome ◽  
Dipeptidyl Aminopeptidase

Nocardia is a complex and diverse genus of aerobic actinomycetes that cause complex clinical presentations, which are difficult to diagnose due to being misunderstood. To date, the genetic diversity, evolution, and taxonomic structure of the genus Nocardia are still unclear. In this study, we investigated the pan-genome of 86 Nocardia type strains to clarify their genetic diversity. Our study revealed an open pan-genome for Nocardia containing 265,836 gene families, with about 99.7% of the pan-genome being variable. Horizontal gene transfer appears to have been an important evolutionary driver of genetic diversity shaping the Nocardia genome and may have caused historical taxonomic confusion from other taxa (primarily Rhodococcus, Skermania, Aldersonia, and Mycobacterium). Based on single-copy gene families, we established a high-accuracy phylogenomic approach for Nocardia using 229 genome sequences. Furthermore, we found 28 potentially new species and reclassified 16 strains. Finally, by comparing the topology between a phylogenomic tree and 384 phylogenetic trees (from 384 single-copy genes from the core genome), we identified a novel locus for inferring the phylogeny of this genus. The dapb1 gene, which encodes dipeptidyl aminopeptidase BI, was far superior to commonly used markers for Nocardia and yielded a topology almost identical to that of genome-based phylogeny. In conclusion, the present study provides insights into the genetic diversity, contributes a robust framework for the taxonomic classification, and elucidates the evolutionary relationships of Nocardia. This framework should facilitate the development of rapid tests for the species identification of highly variable species and has given new insight into the behavior of this genus.

Rapid chromatographic purification of dipeptidyl-aminopeptidase II from human kidney

1987 ◽  
Vol 416 ◽  
pp. 131-137 ◽  
Author(s):  
Toki Sakai ◽  
Kohichi Kojima ◽  
Toshiharu Nagatsu
Keyword(s):  
Human Kidney ◽  
Chromatographic Purification ◽  
Dipeptidyl Aminopeptidase

scholarly journals Purification and Characterization of Dipeptidyl Aminopeptidase fromAureobacteriumsp. WO26

1997 ◽  
Vol 61 (1) ◽  
pp. 146-151 ◽  
Author(s):  
Wataru Ogasawara ◽  
Noriyuki Inanobe ◽  
Keiko Ochiai ◽  
Katsuhiko Ando ◽  
Hirofumi Okada ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Dipeptidyl Aminopeptidase

Intracellular precursors and secretion of alkaline extracellular protease of Yarrowia lipolytica

1988 ◽  
Vol 8 (11) ◽  
pp. 4904-4916
Author(s):  
S Matoba ◽  
J Fukayama ◽  
R A Wing ◽  
D M Ogrydziak
Keyword(s):  
Yarrowia Lipolytica ◽  
Cytoplasmic Membrane ◽  
Extracellular Protease ◽  
Signal Peptidase ◽  
Amino Terminal ◽  
Cell Extracts ◽  
Gene Coding ◽  
Dipeptidyl Aminopeptidase ◽  
Relationship Of ◽  
Yeast Yarrowia Lipolytica

Processing and secretion of the alkaline extracellular protease (AEP) from the yeast Yarrowia lipolytica was studied by pulse-chase and immunoprecipitation experiments. Over half of newly synthesized AEP was secreted by 6 min. Over 99% of AEP activity which was external to the cytoplasmic membrane was located in the supernatant medium. Polypeptides of 55, 52, 44, 36, and 32 kilodaltons (55K, 52K, 44K, 36K, and 32K polypeptides) were immunoprecipitated from [3H]leucine-labeled cell extracts by rabbit antibodies raised against mature, secreted AEP (32K polypeptide). Experiments with tunicamycin and endoglycosidase H indicated that the 55K, 52K, and 44K polypeptides contained about 2 kilodaltons of N-linked oligosaccharide and that the 36K and 32K polypeptides contained none. Results of pulse-chase experiments did not fit a simple precursor-product relationship of 55K----52K----44K----36K----32K. In fact, maximum labeling intensity of the 52K polypeptide occurred later than for the 44K and 36K polypeptides. Secretion of polypeptides of 19 and 20 kilodaltons derived from the proregion of AEP indicated that one major processing pathway was 55K----52K----32K. The gene coding for AEP (XPR2) was cloned and sequenced. The sequence and the immunoprecipitation results suggest that AEP is originally synthesized with an additional preproI-proII-proIII amino-terminal region. Processing definitely involves cleavage(s) after pairs of basic amino acids and the addition of one N-linked oligosaccharide. Signal peptidase cleavage, dipeptidyl aminopeptidase cleavages, and at least one additional proteolytic cleavage may also be involved.

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