1QQJ

CRYSTAL STRUCTURE OF MOUSE FUMARYLACETOACETATE HYDROLASE REFINED AT 1.55 ANGSTROM RESOLUTION

1QQJ の概要

• エントリーDOI: 10.2210/pdb1qqj/pdb
• 関連するPDBエントリー: 1QCN 1QCO
• 分子名称: FUMARYLACETOACETATE HYDROLASE, CALCIUM ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: mixed beta-sandwich roll, hydrolase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92777.28

構造登録者

Timm, D.E.,Mueller, H.A.,Bhanumoorthy, P.,Harp, J.M.,Bunick, G.J. (登録日: 1999-06-07, 公開日: 2000-06-07, 最終更新日: 2024-02-14)

主引用文献

Timm, D.E.,Mueller, H.A.,Bhanumoorthy, P.,Harp, J.M.,Bunick, G.J.
Crystal structure and mechanism of a carbon-carbon bond hydrolase.
Structure Fold.Des., 7:1023-1033, 1999

PubMed Abstract: Fumarylacetoacetate hydrolase (FAH) catalyzes the final step of tyrosine and phenylalanine catabolism, the hydrolytic cleavage of a carbon-carbon bond in fumarylacetoacetate, to yield fumarate and acetoacetate. FAH has no known sequence homologs and functions by an unknown mechanism. Carbon-carbon hydrolysis reactions are essential for the human metabolism of aromatic amino acids. FAH deficiency causes the fatal metabolic disease hereditary tyrosinemia type I. Carbon-carbon bond hydrolysis is also important in the microbial metabolism of aromatic compounds as part of the global carbon cycle.

PubMed: 10508789
DOI: 10.1016/S0969-2126(99)80170-1

実験手法

X-RAY DIFFRACTION (1.55 Å)