1CHU

STRUCTURE OF L-ASPARTATE OXIDASE: IMPLICATIONS FOR THE SUCCINATE DEHYDROGENASE/ FUMARATE REDUCATSE FAMILY

Summary for 1CHU

• Entry DOI: 10.2210/pdb1chu/pdb
• Descriptor: PROTEIN (L-ASPARTATE OXIDASE) (2 entities in total)
• Functional Keywords: flavoenzyme, nad biosynthesis, fad, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P10902
• Total number of polymer chains: 1
• Total formula weight: 60430.33

Authors

Mattevi, A. (deposition date: 1999-03-29, release date: 1999-06-23, Last modification date: 2023-12-27)

Primary citation

Mattevi, A.,Tedeschi, G.,Bacchella, L.,Coda, A.,Negri, A.,Ronchi, S.
Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.
Structure Fold.Des., 7:745-756, 1999

PubMed Abstract: Given the vital role of NAD+ in cell metabolism, the enzymes involved in bacterial de novo NAD+ biosynthesis are possible targets for drug design against pathogenic bacteria. The first reaction in the pathway is catalysed by L-aspartate oxidase (LASPO), a flavoenzyme that converts aspartate to iminoaspartate using either molecular oxygen or fumarate as electron acceptors. LASPO has considerable sequence homology with the flavoprotein subunits of succinate dehydrogenase (SDH) and fumarate reductase (FRD).

PubMed: 10425677
DOI: 10.1016/S0969-2126(99)80099-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)