Effects of Truncation at the Non-homologous Region of a Family 3 β-Glucosidase from Agrobacterium tumefaciens
スポンサーリンク
概要
- 論文の詳細を見る
The function of the non-homologous region of a family 3 β-glucosidase from Agrobacterium tumefaciens (Cbg1) was studied by analyzing the properties of mutant enzymes that have internal truncated amino acid sequences in the region. Five truncated mutants named Cbg1-d4, Cbg1-d31, Cbg1-d62, Cbg1-d89, and Cbg1-d119 having deletions of 4, 31, 62, 89, and 119 amino acid residues starting from Phe417, respectively, were expressed in Escherichia coli and purified. All the mutants exhibited β-glucosidase activity, indicating that the non-homologous region was not essential for the activity. The truncation caused thermal instability, decrease in pKa of the proton donor residue (Glu616), and deficient transglycosylation activity. The thermal stability and the pKa of Glu616 were partially recovered with longer truncation, suggesting that the truncation perturbed the structure and that their presence in the region was not essential. The main role of the non-homologous region could be formation of a hydrophobic atmosphere at the acceptor site to make the enzyme suitable for hydrolyzing hydrophobic glucosides.
- 社団法人 日本農芸化学会の論文
- 2004-05-23
著者
-
Kitaoka Motomitsu
National Food Research Institute, National Agriculture and Food Research Organization
-
KITAOKA Motomitsu
Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organiza
-
Kitaoka M
Enzyme Laboratory National Food Research Institute
-
Kitaoka M
Chubu Univ. Aichi Jpn
-
Kitaoka Motomitsu
Enzyme Laboratory National Food Research Institute National Agriculture And Food Research Organizati
-
HAYASHI Kiyoshi
Enzyme Applications Laboratory, National Food Research Institute
-
Kitaoka Motomitsu
Enzyme Laboratory National Food Research Institute
-
LI YING
Enzyme Laboratory, National Food Research Institute
-
Li Ying
Enzyme Laboratory National Food Research Institute
-
Ying Li
Enzyme Laboratory National Food Research Institute National Agriculture And Food Research Organizati
-
Hayashi Kiyoshi
Enzyme Laboratory National Food Research Institute National Agriculture And Food Research Organization
関連論文
- Practical Preparation of D-Galactosyl-β1→4-L-rhamnose Employing the Combined Action of Phosphorylases
- Analyses of Bifidobacterial Glycosidases Involved in the Metabolism of Oligosaccharides
- The Role of Conserved Arginine Residue in Loop 4 of Glycoside Hydrolase Family 10 Xylanases
- Crystallographic and Mutational Analyses of Substrate Recognition of Endo-α-N-acetylgalactosaminidase from Bifidobacterium longum
- グライコシンターゼ化による反転型加水分解酵素のグリコシド合成触媒への変換
- Kinetic Studies on p-Nitrophenyl-cellobioside Hydrolyzing Xylanase from Cellvibrio gilvus
- Phosphorolytic Reaction of Cellvibrio gilvus Cellobiose Phosphorylase
- Purification and Properties of a Xylanase from Cellvibrio gilvus That Hydrolyzes p-Nitrophenyl Cellooligosaccharides(Biological Chemistry)
- Synthesis of Laminarioligosaccharides Using Crude Extract of Euglena gracilis z Cells(Biological Chemistry)
- A Simple Method of Cellulase Immobilization on a Modified Silica Support
- Purification and Characterization of Extracellular Chitin Deacetylase from Colletotrichum lindemuthianum
- 647 A putative proline iminopeptidase of Thermotoga maritime with leucine- and lysine-p-nitroanilide hydrolyzing activities
- Practical Preparation of Lacto-N-biose I, a Candidate for the Bifidus Factor in Human Milk
- Characterization of a Cellobiose Phosphorylase from a Hyperthermophilic Eubacterium, Thermotoga maritima MSB8(Biochemistry & Molecular Biology)
- Kinetic Studies of a Recombinant Cellobiose Phosphorylase (CBP) of the Clostridium thermocellum YM4 Strain Expressed in Escherichia coli
- Effects of Truncation at the Non-homologous Region of a Family 3 β-Glucosidase from Agrobacterium tumefaciens
- Identification of the Putative Proton Donor Residue of Lacto-N-biose Phosphorylase (EC 2.4.1.211)
- A Thermostable Non-xylanolytic α-Glucuronidase of Thermotoga maritima MSB8(Biochemistry & Molecular Biology)
- Syntheses of 4-Methylumbelliferyl-β-D-Xylobioside and 5-Bromo-3-Indolyl-β-D-Xylobioside for Sensitive Detection of Xylanase Activity on Agar Plates
- Diversity and Similarity of Microbial Communities in Petroleum Crude Oils Produced in Asia
- Characterization of Bacillus halodurans α-Galactosidase Mel4A Encoded by the mel4A Gene (BH2228)
- Characterization of a Thermostable Family 10 Endo-Xylanase (XynB) from Thermotoga maritima That Cleaves p-Nitrophenyl-β-D-Xlyloside
- Analyses of Bifidobacterial Glycosidases Involved in the Metabolism of Oligosaccharides
- 糖質加リン酸分解酵素
- Kinetic Studies on the Hydrolysis of N-Acetylated and N-Deacetylated Derivatives of 4-Methylumbelliferyl Chitobioside by the Family 18 Chitinases ChiA and ChiB from Serratia Marcescens
- Substrate Specificity of the N, 6-ο-Diacetylmuramidase from Streptomyces globisporus
- An Investigation of the pH-Activity Relationships of Cex, a Family 10 Xylanase from Cellulomonas fimi : Xylan Inhibition and the Influence of Nitro-Substituted Aryl-β-D-Xylobiosides on Xylanase Activity
- グライコシンターゼ化による反転型加水分解酵素のグリコシド合成触媒への変換
- Controlled Nanophase Development in Photocatalytic Titania
- Prebiotic Effect of Lacto-N-biose I on Bifidobacterial Growth
- Characterization of Bacillus halodurans α-Galactosidase Me14A Encoded by the mel4A Gene (BH2228)
- Practical Preparation of D-Galactosyl-β1→4-L-rhamnose Employing the Combined Action of Phosphorylases
- Molecular Anatomy of the Alkaliphilic Xylanase from Bacillus halodurans C-125
- Employing Chimeric Xylanases to Identify Regions of an Alkaline Xylanase Participating in Fnzyme Activity at Basic pH(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Structural Explanation for the Acquisition of Glycosynthase Activity
- A Kinetic Study on pH-Activity Relationship of XynA from Alkaliphilic Bacillus halodurans C-125 Using Aryl-Xylobiosides
- Characterization of N-Acetylmuramidase M-1 of Streptomyces globisporus Produced by Escherichia coli BL21(DE3)pLysS
- Characterization of Glycosynthase Mutants Derived from Glycoside Hydrolase Family 10 Xylanases
- Mutational Analysis of Fungal Family 11 Xylanases on pH Optimum Determination
- Interactions between Glycoside Hydrolase Family 94 Cellobiose Phosphorylase and Glucosidase Inhibitors
- p-Nitrophenyl β-Glycosides of β-1,4-Gluco/xylo-disaccharides for the Characterization of Subsites in Endo-xylanases
- Self-transferring Product Inhibition Observed during the Hydrolysis of Aryl-β-D-Glucopyranosides by a β-Glucosidase from Agrobacterium tumefaciens
- Characterization of a Bacterial Laminaribiose Phosphorylase