دورية أكاديمية
The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli.
| العنوان: | The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. |
|---|---|
| المؤلفون: | Izard T; Biomolecular Research Institute, Parkville, Australia., Lawrence MC, Malby RL, Lilley GG, Colman PM |
| المصدر: | Structure (London, England : 1993) [Structure] 1994 May 15; Vol. 2 (5), pp. 361-9. |
| نوع المنشور: | Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print Cited Medium: Print ISSN: 0969-2126 (Print) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2000- : Cambridge, Mass. : Cell Press Original Publication: London : Current Biology, c1993- |
| مواضيع طبية MeSH: | Escherichia coli/*enzymology , Oxo-Acid-Lyases/*chemistry, Aldehyde-Lyases/chemistry ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; N-Acetylneuraminic Acid ; Protein Conformation ; Sequence Homology, Amino Acid ; Sialic Acids/metabolism |
| مستخلص: | Background: N-acetylneuraminate lyase catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. The enzyme plays an important role in the regulation of sialic acid metabolism in bacteria. The reverse reaction can be exploited for the synthesis of sialic acid and some of its derivatives. Results: The structure of the enzyme from Escherichia coli has been determined to 2.2 A resolution by X-ray crystallography. The enzyme is shown to be a tetramer, in which each subunit consists of an alpha/beta-barrel domain followed by a carboxy-terminal extension of three alpha-helices. Conclusions: The active site of the enzyme is tentatively identified as a pocket at the carboxy-terminal end of the eight-stranded beta-barrel. Lys165 lies within this pocket and is probably the reactive residue which forms a Schiff base intermediate with the substrate. The sequence of N-acetylneuraminate lyase has similarities to those of dihydrodipicolinate synthase and MosA (an enzyme implicated in rhizopine synthesis) suggesting that these last two enzymes share a similar structure to N-acetylneuraminate lyase. |
| المشرفين على المادة: | 0 (Sialic Acids) EC 4.1.2.- (Aldehyde-Lyases) EC 4.1.3.- (Oxo-Acid-Lyases) EC 4.1.3.3 (N-acetylneuraminate lyase) GZP2782OP0 (N-Acetylneuraminic Acid) |
| تواريخ الأحداث: | Date Created: 19940515 Date Completed: 19941011 Latest Revision: 20190914 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/s0969-2126(00)00038-1 |
| PMID: | 8081752 |
| قاعدة البيانات: | MEDLINE |
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