1QCO

CRYSTAL STRUCTURE OF FUMARYLACETOACETATE HYDROLASE COMPLEXED WITH FUMARATE AND ACETOACETATE

Summary for 1QCO

• Entry DOI: 10.2210/pdb1qco/pdb
• Related: 1QCN 1QQJ
• Descriptor: FUMARYLACETOACETATE HYDROLASE, CALCIUM ION, NICKEL (II) ION, ... (6 entities in total)
• Functional Keywords: mixed beta sandwich roll, hydrolase
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 93691.52

Authors

Timm, D.E.,Mueller, H.A.,Bhanumoorthy, P.,Harp, J.M.,Bunick, G.J. (deposition date: 1999-05-17, release date: 2000-06-07, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)