1E5Q

Ternary complex of saccharopine reductase from Magnaporthe grisea, NADPH and saccharopine

Summary for 1E5Q

• Entry DOI: 10.2210/pdb1e5q/pdb
• Related: 1E5L
• Descriptor: Saccharopine dehydrogenase [NADP(+), L-glutamate-forming], NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, N-(5-AMINO-5-CARBOXYPENTYL)GLUTAMIC ACID, ... (4 entities in total)
• Functional Keywords: oxidoreductase, saccharopine reductase, nadph, lysine biosynthesis, alpha- aminoadipate pathway
• Biological source: Magnaporthe oryzae (Rice blast fungus)
• Total number of polymer chains: 8
• Total formula weight: 401423.75

Authors

Johansson, E.,Steffens, J.J.,Lindqvist, Y.,Schneider, G. (deposition date: 2000-07-28, release date: 2000-12-03, Last modification date: 2023-12-13)

Primary citation

Johansson, E.,Steffens, J.J.,Lindqvist, Y.,Schneider, G.
Crystal Structure of Saccharopine Reductase from Magnaporthe Grisea, an Enzyme of the Alpha-Aminoadipate Pathway of Lysine Biosynthesis
Structure, 8:1037-, 2000

PubMed Abstract: The biosynthesis of the essential amino acid lysine in higher fungi and cyanobacteria occurs via the alpha-aminoadipate pathway, which is completely different from the lysine biosynthetic pathway found in plants and bacteria. The penultimate reaction in the alpha-aminoadipate pathway is catalysed by NADPH-dependent saccharopine reductase. We set out to determine the structure of this enzyme as a first step in exploring the structural biology of fungal lysine biosynthesis.

PubMed: 11080625
DOI: 10.1016/S0969-2126(00)00512-8

Experimental method

X-RAY DIFFRACTION (2.1 Å)