1CD5
GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER
1CD5 の概要
| エントリーDOI | 10.2210/pdb1cd5/pdb |
| 分子名称 | PROTEIN (GLUCOSAMINE 6-PHOSPHATE DEAMINASE) (2 entities in total) |
| 機能のキーワード | allosteric enzyme, entropic effects, aldose-ketose isomerase, isomerase |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 29812.21 |
| 構造登録者 | Horjales, E.,Altamirano, M.M.,Calcagno, M.L.,Garratt, R.C.,Oliva, G. (登録日: 1999-03-05, 公開日: 2000-03-06, 最終更新日: 2023-08-09) |
| 主引用文献 | Horjales, E.,Altamirano, M.M.,Calcagno, M.L.,Garratt, R.C.,Oliva, G. The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution. Structure Fold.Des., 7:527-537, 1999 Cited by PubMed Abstract: The allosteric hexameric enzyme glucosamine-6-phosphate deaminase from Escherichia coli catalyses the regulatory step of N-acetylglucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia. The reversibility of the catalysis and its rapid-equilibrium random kinetic mechanism, among other properties, make this enzyme a good model for studying allosteric processes. PubMed: 10378272DOI: 10.1016/S0969-2126(99)80069-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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