Download MendeleyThe initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase.
Faehnle, C.R., Liu, X., Pavlovsky, A., Viola, R.E.(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 962-966
- PubMed: 17012784
- DOI: https://doi.org/10.1107/S1744309106038279
- Primary Citation of Related Structures:
2HMF - PubMed Abstract:
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.
Organizational Affiliation:
Department of Chemistry, University of Toledo, Toledo, Ohio 43606, USA.
