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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/07/14 07:18:02」(JST)
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English Journal
- Functional and structural analysis of the major amidase (Atl) in Staphylococcus.
- Götz F1, Heilmann C2, Stehle T3.Author information 1Microbial Genetics, Interfaculty Institute for Microbiology and Infection Medicine Tübingen (IMIT), University of Tübingen, 72076 Tübingen, Germany. Electronic address: friedrich.goetz@uni-tuebingen.de.2Institute for Medical Microbiology, University Hospital Münster, Domagkstrasse 10, 48149 Münster, Germany.3Interfaculty Institute of Biochemistry, University of Tübingen, Hoppe-Seyler-Straße 4, 72076 Tübingen, Germany; Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.AbstractThe cytoplasmic membrane of most bacteria is surrounded by a more or less thick murein layer (peptidoglycan) that protects the protoplast from mechanical damage, osmotic rupture and lysis. When bacteria are dividing processes are initiated stepwise that involve DNA replication, constriction of the membranes, cell growth, biosynthesis of new murein, and finally the generation of two daughter cells. As the daughter cells are still covalently interlinked by the murein network they must be separated by specific peptidoglycan hydrolases, also referred to as autolysins. In staphylococci, the major autolysin (Atl) and its processed products N-acetylmuramoyl-l-alanine amidase (AM) and endo-β-N-acetylglucosaminidase (GL) have been in the research focus for long time. This review addresses phenotypic consequences of atl mutants, impact of Atl in virulence, the mechanism of targeting to the septum region, regulation of atl, the structure of the amidase and the repeat regions, as well as the phylogeny of Atl and its use in Staphylococcus genus and species typing.
- International journal of medical microbiology : IJMM.Int J Med Microbiol.2014 Mar;304(2):156-63. doi: 10.1016/j.ijmm.2013.11.006. Epub 2013 Dec 1.
- The cytoplasmic membrane of most bacteria is surrounded by a more or less thick murein layer (peptidoglycan) that protects the protoplast from mechanical damage, osmotic rupture and lysis. When bacteria are dividing processes are initiated stepwise that involve DNA replication, constriction of the m
- PMID 24444718
- Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis.
- Zhang Q1, Marsolais F2.Author information 1Department of Biology, University of Western Ontario, London, ON N6A 5B7, Canada; Agriculture and Agri-Food Canada, Genomics and Biotechnology, Southern Crop Protection and Food Research Centre, 1391 Sandford St., London, ON N5V 4T3, Canada.2Department of Biology, University of Western Ontario, London, ON N6A 5B7, Canada; Agriculture and Agri-Food Canada, Genomics and Biotechnology, Southern Crop Protection and Food Research Centre, 1391 Sandford St., London, ON N5V 4T3, Canada. Electronic address: Frederic.Marsolais@agr.gc.ca.AbstractIn higher plants, asparagine (Asn) is a major form of organic nitrogen used for transport and storage. There are two pathways of Asn metabolism, involving asparaginase and Asn aminotransferase. The enzyme serine:glyoxylate aminotransferase encoded by AGT1 has been identified as an asparagine aminotransferase in Arabidopsis. The product of asparagine transamination, alpha-ketosuccinamate, can be hydrolyzed by the enzyme omega-amidase to form oxaloacetate and ammonia. A candidate gene was identified in Arabidopsis based on its sequence similarity with mouse omega-amidase. Recombinant omega-amidase exhibited comparable catalytic activities with alpha-hydroxysuccinamate, alpha-ketosuccinamate and alpha-ketoglutaramate, the product of glutamine transamination. A mutant with a T-DNA inserted in the first exon accumulated alpha-ketosuccinamate and alpha-hydroxysuccinamate as compared with wild-type, both under control conditions and after treatment with Asn. Treatment with Asn led to decreased transcript levels of omega-amidase in root, while transcript levels of AGT1 are increased under these conditions, suggesting that excess Asn may lead to the accumulation of alpha-ketosuccinamate and alpha-hydroxysuccinamate.
- Phytochemistry.Phytochemistry.2014 Mar;99:36-43. doi: 10.1016/j.phytochem.2013.12.020. Epub 2014 Jan 22.
- In higher plants, asparagine (Asn) is a major form of organic nitrogen used for transport and storage. There are two pathways of Asn metabolism, involving asparaginase and Asn aminotransferase. The enzyme serine:glyoxylate aminotransferase encoded by AGT1 has been identified as an asparagine aminotr
- PMID 24461228
- Repeating structures of the major staphylococcal autolysin are essential for the interaction with human thrombospondin 1 and vitronectin.
- Kohler TP1, Gisch N, Binsker U, Schlag M, Darm K, Völker U, Zähringer U, Hammerschmidt S.Author information 1From the Department of Genetics of Microorganisms and.AbstractHuman thrombospondin 1 (hTSP-1) is a matricellular glycoprotein facilitating bacterial adherence to and invasion into eukaryotic cells. However, the bacterial adhesin(s) remain elusive. In this study, we show a dose-dependent binding of soluble hTSP-1 to Gram-positive but not Gram-negative bacteria. Diminished binding of soluble hTSP-1 to proteolytically pretreated staphylococci suggested a proteinaceous nature of potential bacterial adhesin(s) for hTSP-1. A combination of separation of staphylococcal surface proteins by two-dimensional gel electrophoresis with a ligand overlay assay with hTSP-1 and identification of the target protein by mass spectrometry revealed the major staphylococcal autolysin Atl as a bacterial binding protein for hTSP-1. Binding experiments with heterologously expressed repeats of the AtlE amidase from Staphylococcus epidermidis suggest that the repeating sequences (R1ab-R2ab) of the N-acetyl-muramoyl-l-alanine amidase of Atl are essential for binding of hTSP-1. Atl has also been identified previously as a staphylococcal vitronectin (Vn)-binding protein. Similar to the interaction with hTSP-1, the R1ab-R2ab repeats of Atl are shown here to be crucial for the interaction of Atl with the complement inhibition and matrix protein Vn. Competition assays with hTSP-1 and Vn revealed the R1ab-R2ab repeats of AtlE as the common binding domain for both host proteins. Furthermore, Vn competes with hTSP-1 for binding to Atl repeats and vice versa. In conclusion, this study identifies the Atl repeats as bacterial adhesive structures interacting with the human glycoproteins hTSP-1 and Vn. Finally, this study provides insight into the molecular interplay between hTSP-1 and Vn, respectively, and a bacterial autolysin.
- The Journal of biological chemistry.J Biol Chem.2014 Feb 14;289(7):4070-82. doi: 10.1074/jbc.M113.521229. Epub 2013 Dec 26.
- Human thrombospondin 1 (hTSP-1) is a matricellular glycoprotein facilitating bacterial adherence to and invasion into eukaryotic cells. However, the bacterial adhesin(s) remain elusive. In this study, we show a dose-dependent binding of soluble hTSP-1 to Gram-positive but not Gram-negative bacteria.
- PMID 24371140
Japanese Journal
- 3S-Dp03 Quorum Sensing シグナル物質分解遺伝子の多様性と応用(若手が切り拓くBiofilm/cell-cell communication研究の新展開,シンポジウム)
- 日本生物工学会大会講演要旨集 66, 188, 2014
- NAID 110009906669
- 1P-079 L-ピペコリン酸アシラーゼ生産菌の探索と諸性質の検討(酵素学,酵素工学,一般講演)
- 日本生物工学会大会講演要旨集 66, 37, 2014
- NAID 110009906160
- Production and Degradation of <i>N</i>-Acylhomoserine Lactone Quorum Sensing Signal Molecules in Bacteria Isolated from Activated Sludge
- Bioscience, Biotechnology, and Biochemistry 77(12), 2436-2440, 2013
- NAID 130003381962
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- acylase 【名】《化》アシラーゼ - アルクがお届けする進化するオンライン英和・和英辞書データベース。一般的な単語や連語から、イディオム、専門用語、スラングまで幅広く収録。
- acylase /ac·yl·ase/ (a´sĭ-lās) amidase (1). ac·yl·ase (ăs′ə-lās′, -lāz′) n. See amidase. acylase (1) Amidase, EC 3.5.1.4 (Acylamide amidohydrolase). ... Disclaimer All content on this website, including dictionary, thesaurus, literature ...
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★リンクテーブル★
| リンク元 | 「acylamidase」「アシラーゼ」 |
| 拡張検索 | 「transacylase」「aspartoacylase」 |