The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase.
The activation of the beta-carboxyl group of aspartate catalyzed by aspartokinase is the commitment step to amino-acid biosynthesis in the aspartate pathway. The first structure of a microbial aspartokinase, that from Methanococcus jannaschii, has been determined in the presence of the amino-acid substrate L-aspartic acid and the nucleotide product MgADP. The enzyme assembles into a dimer of dimers, with the interfaces mediated by both the N- and C-terminal domains. The active-site functional groups responsible for substrate binding and specificity have been identified and roles have been proposed for putative catalytic functional groups.
Faehnle
Christopher R
CR
Department of Chemistry, University of Toledo, Toledo, Ohio 43606, USA.
Liu
Xuying
X
Pavlovsky
Alexander
A
Viola
Ronald E
RE
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D001222:Aspartate Kinase / Q000737:chemistry* / Q000378:metabolism; D001224:Aspartic Acid / Q000096:biosynthesis*; D001665:Binding Sites; D002384:Catalysis; D025461:Feedback, Physiological; D017017:Methanococcus / Q000737:chemistry / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
D019843:Archaeal Proteins; D021122:Protein Subunits; D001224:Aspartic Acid; D001222:Aspartate Kinase