title: Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
abstract: LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of α-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection of AAA but also uses LysW to protect the amino group of glutamate in arginine biosynthesis. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. The crystal structure of ArgX, the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW, was determined in complex with LysW. Structural comparison and enzymatic characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX identify the amino acid motif responsible for substrate discrimination between AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at different stages of evolution led to ArgX and LysX.
authors: Biotechnology Research Center, The University of Tokyo, Tokyo, Japan.
authors: Takuya
authors: T
authors: Ouchi
authors: Takeo
authors: T
authors: Tomita
authors: Akira
authors: A
authors: Horie
authors: Ayako
authors: A
authors: Yoshida
authors: Kento
authors: K
authors: Takahashi
authors: Hiromi
authors: H
authors: Nishida
authors: Kerstin
authors: K
authors: Lassak
authors: Hikari
authors: H
authors: Taka
authors: Reiko
authors: R
authors: Mineki
authors: Tsutomu
authors: T
authors: Fujimura
authors: Saori
authors: S
authors: Kosono
authors: Chiharu
authors: C
authors: Nishiyama
authors: Ryoji
authors: R
authors: Masui
authors: Seiki
authors: S
authors: Kuramitsu
authors: Sonja-Verena
authors: SV
authors: Albers
authors: Tomohisa
authors: T
authors: Kuzuyama
authors: Makoto
authors: M
authors: Nishiyama
mesh_terms: D015074:2-Aminoadipic Acid / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001120:Arginine / Q000096:biosynthesis*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D019143:Evolution, Molecular; D020440:Gene Duplication; D018698:Glutamic Acid / Q000378:metabolism; D008239:Lysine / Q000096:biosynthesis*; D008958:Models, Molecular; D009952:Ornithine / Q000378:metabolism; D010802:Phylogeny; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D016945:Sulfolobus acidocaldarius / Q000235:genetics / Q000378:metabolism*; D013824:Thermus / Q000235:genetics / Q000378:metabolism
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D011994:Recombinant Proteins; D015074:2-Aminoadipic Acid; D018698:Glutamic Acid; D001120:Arginine; D009952:Ornithine; D008239:Lysine