6ald: Difference between revisions
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Revision as of 18:44, 30 October 2007
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RABBIT MUSCLE ALDOLASE A/FRUCTOSE-1,6-BISPHOSPHATE COMPLEX
OverviewOverview
Class I fructose-1,6-bis(phosphate) aldolase is a glycolytic enzyme that, catalyzes the cleavage of fructose 1,6-bis(phosphate) through a covalent, Schiff base intermediate. Although the atomic structure of this enzyme is, known, assigning catalytic roles to the various enzymic active-site, residues has been hampered by the lack of a structure for the, enzyme-substrate complex. A mutant aldolase, K146A, is unable to cleave, the C3-C4 bond of the hexose while retaining the ability to form the, covalent intermediate, although at a greatly diminished rate. The, structure of rabbit muscle K146A-aldolase A, in complex with its native, substrate, fructose 1,6-bis(phosphate), is determined to 2.3 A resolution, by molecular replacement. The density at the hexose binding site differs, between ... [(full description)]
About this StructureAbout this Structure
6ALD is a [Single protein] structure of sequence from [Oryctolagus cuniculus] with 2FP as [ligand]. Active as [Fructose-bisphosphate aldolase], with EC number [4.1.2.13]. Structure known Active Sites: CAT and CTB. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,)., Choi KH, Mazurkie AS, Morris AJ, Utheza D, Tolan DR, Allen KN, Biochemistry. 1999 Sep 28;38(39):12655-64. PMID:10504235
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