ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLIASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI
Structural highlights
1brm is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
DHAS_ECOLI Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Biellmann JF, Eid P, Hirth C, Jornvall H. Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties. Eur J Biochem. 1980 Feb;104(1):53-8. PMID:6102909
↑Chassagnole C, Rais B, Quentin E, Fell DA, Mazat JP. An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. Biochem J. 2001 Jun 1;356(Pt 2):415-23. PMID:11368768
