1ALD

ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES

Summary for 1ALD

• Entry DOI: 10.2210/pdb1ald/pdb
• Descriptor: ALDOLASE A (1 entity in total)
• Functional Keywords: lyase (aldehyde)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, myofibril, sarcomere, I band: P04075
• Total number of polymer chains: 1
• Total formula weight: 39338.78

Authors

Watson, H.C. (deposition date: 1991-05-05, release date: 1992-01-15, Last modification date: 2024-02-07)

Primary citation

Gamblin, S.J.,Davies, G.J.,Grimes, J.M.,Jackson, R.M.,Littlechild, J.A.,Watson, H.C.
Activity and specificity of human aldolases.
J.Mol.Biol., 219:573-576, 1991

PubMed Abstract: The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.

PubMed: 2056525
DOI: 10.1016/0022-2836(91)90650-U

Experimental method

X-RAY DIFFRACTION (2 Å)