Subsite Structure and Mode of Action of Native and Modified α-Amylase from Poricine Pancreas(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
The subsite structure of an active component of porcine pancreatic α-amylase, called PPA II, and modified PPA II (M_2) obtained with 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), were setimated from their mode of action and rate parameters of hydrolyses of maltooligosaccharides. These results indicated that the native and modified PPA II have five subsites withe the catalytic site located between the third and fourth subsites from the nonreducing end. The subsite structure calculated for M_2 differed from that of PPA II; subsite affinities of PPA II were calculated to be 1.6, 3.9 and 2.8 kcal/mol for subsites 1, 2 and 5, respectively, whereas corresponding values for M_2 were 1.5, 1.4 and 2.6 kcal/mol, respectively. The sum of affinities of the third and fourth subsites was calculated to be -3.6 kcal/mol for PPA II and -2.1 kcal/mol for M_2, respectively, Evidently the mode of action of PPA II was changed by the introduction of bulky TNB^- ion at or near subsite 2. The difference of the mode of action between PPA II and M_2 was interpreted in terms of the structure of each subsite.
- 社団法人日本農芸化学会の論文
- 1986-12-23
著者
-
Kobayashi Toshitaka
Central Research Institute Meiji Milk Products Co. Ltd.
-
Kobayashi T
Nagoya Univ. Nagoya Jpn
-
SAKANO Yoshiyuki
Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, To
-
ISHIZUKA Yasuyuki
Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, To
-
KOBAYASHI Tsuneo
Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, To
-
Ishizuka Yasuyuki
Laboratory Of Biological Chemistry Department Of Agricultural Chemistry Faculty Of Agriculture Tokyo
-
Sakano Y
Department Of Applied Biological Science Faculty Of Agriculture Tokyo University Of Agriculture And
-
Sakano Yoshiyuki
Laboratory Of Biochemistry Department Of Agricultural Chemistry Tokyo University Of Agriculture And
関連論文
- Structures of Thermoactinomyces vulgaris R-47 α-Amylase II Complexed with Substrate Analogues
- The Deletion of Amino-Terminal Domain in Thermoactinomyces vulgaris R-47 α-Amylases : Effects of domain N on Activity, Specificity, Stability and Dimerization
- Analysis of Catalytic Residues of Thermoactinomyces vulgaris R-47 α-Amylase II (TVA II) by Site-directed Mutagenesis
- Purification, Characterization, and Subsite Affinities of Thermoactinomyces vulgaris R-47 Maltooligosaccharide-metabolizing Enzyme Homologous to Glucoamylases
- Construction of an Efficient Expression System for Aspergillus Isopullulanase in Pichia pastoris, and a Simple Purification Method(Biochemistry & Molecular Biology)
- Studies on the Hydrolyzing Mechanism for Cyclodextrins of Thermoactinomyces vulgaris R-47 α-Amylase 2 (TVAII). X-Ray Structure of the Mutant E354A Complexed with β-Cyclodextrin, and Kinetic Analyses on Cyclodextrins
- Enzymatic Deglycation of Fructosyl-lysine(Biological Chemistry)
- Chemical Modification of Sulfhydryl Groups in Porcine Pancreatic α-Amylase, and Purification and Properties of the Modified Amylase(Biological Chemistry)
- Subsite Structure and Mode of Action of Native and Modified α-Amylase from Poricine Pancreas(Biological Chemistry)
- ^Na-NMR Imaging of Foods(Analytical Chemistry)
- Quality Control of Extruded Jelly through a Predicted Enthalpy Profile(Food & Nutrition)
- Estimation of the Enthalpy Profile of Food Materials in a Twin-screw Extruder(Food & Nutrition)
- Tracing Metabolic Changes in Soybean Cotyledons during Germination by NMR(Biological Chemistry)
- Pumping Characteristic of a Twin-screw Extruder(Food & Nutrition)
- ^1H-NMR Imaging of Tomato Fruits(Biological Chemistry)
- Analysis of Physical States of Water in Soybean Seeds by NMR(Biological Chemistry)
- The Relationship between Imbibitional Damage and Initial Water Content of Soybeans(Biological Chemistry)
- Estimation of Biological Activities by NMR in Soybean Seeds during Maturation(Biological Chemistry)
- Reddish Escherichia coli Cells Caused by Overproduction of Bacillus stearothermophilus Uroporphyrinogen III Methylase : Cloning, Sequencing, and Expression of the Gene
- A Neopullulanase-type α-Amylase Gene from Thermoactinomyces vulgaris R-47
- Immobilization of Bacillus acidopullulyticus Pullulanase and Properties of the Immobilized Pullulanases
- Synthesis of Maltosyl(α1→6)cyclodextrins through the Reverse Reaction of Thermostable Bacillus acidopullulyticus Pullulanase(Biological Chemistry)
- Purification and Properties of Bacillus acidopullulyticus Pullulanase (Biological Chemistry)
- Synthesis of Branched α-Cyclodextrin Carrying a Side Chain Longer than Maltose Using Bacillus acidopullulyticus Pullulanase(Biological Chemistry)
- Uptake of ^3H-Cortisol by Isolated Liver Nuclei Obtained from Hypophysectomized Rat
- Preparation and Enzymatic Hydrolysis of Maltosyl-α-cyclodextrin
- The mineral nutrition of cultured chlorophyllous cells of tobacco I. Effects of πsalts, πsucrose, Ca, Cl and B in the medium on the yield, friability, chlorophyll contents and mineral absorption of cells
- Purification and Properties of an exo-α-Amylase from Pseudomonas stutzeri
- Purification of a-Maltotetraose-forming exo-Amylase of Pseudomonas stutzeri-Two-forms of the Amylase and Their Enzymatic Properties
- Hydrolysis of α-1, 4- and α-1, 6-Glucosidic Linkages in Trisaccharides by the Thermoactinomyces vulgaris α-Amylase
- Hydrolysis of α-1, 6-Glucosidic Linkages by α-Amylases