1JEN

HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE

1JEN の概要

• エントリーDOI: 10.2210/pdb1jen/pdb
• 分子名称: PROTEIN (S-ADENOSYLMETHIONINE DECARBOXYLASE (BETA CHAIN)), PROTEIN (S-ADENOSYLMETHIONINE DECARBOXYLASE (ALPHA CHAIN)) (3 entities in total)
• 機能のキーワード: s-adenosylmethionine decarboxylase, pyruvoyl, gene duplication, polyamine biosynthesis, sandwich, allosteric enzyme
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76933.36

構造登録者

Ekstrom, J.L.,Mathews, I.I.,Stanley, B.A.,Pegg, A.E.,Ealick, S.E. (登録日: 1999-02-23, 公開日: 1999-06-01, 最終更新日: 2023-11-15)

主引用文献

Ekstrom, J.L.,Mathews, I.I.,Stanley, B.A.,Pegg, A.E.,Ealick, S.E.
The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold.
Structure Fold.Des., 7:583-595, 1999

PubMed Abstract: S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine synthetic pathway, and a well-studied drug target. The AdoMetDC decarboxylation reaction depends upon a pyruvoyl cofactor generated via an intramolecular proenzyme self-cleavage reaction. Both the proenzyme-processing and substrate-decarboxylation reactions are allosterically enhanced by putrescine. Structural elucidation of this enzyme is necessary to fully interpret the existing mutational and inhibitor-binding data, and to suggest further experimental studies.

PubMed: 10378277
DOI: 10.1016/S0969-2126(99)80074-4

実験手法

X-RAY DIFFRACTION (2.25 Å)