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Threshold in a single enzyme reaction system. Reaction of maltose catalyzed by saccharifying alpha-amylase from B. subtilis.

作者信息

Matsuno R, Nakanishi K, Ohnishi M, Hiromi K, Kamikubo T

出版信息

J Biochem. 1978 Mar;83(3):859-62. doi: 10.1093/oxfordjournals.jbchem.a131982.

DOI:10.1093/oxfordjournals.jbchem.a131982
PMID:417077
Abstract
摘要

相似文献

1
Threshold in a single enzyme reaction system. Reaction of maltose catalyzed by saccharifying alpha-amylase from B. subtilis.单一酶反应体系中的阈值。枯草芽孢杆菌糖化α-淀粉酶催化麦芽糖的反应。
J Biochem. 1978 Mar;83(3):859-62. doi: 10.1093/oxfordjournals.jbchem.a131982.
2
Reaction mechanism of saccharifying alpha-amylase from B. subtilis with maltose as a substrate.以麦芽糖为底物时枯草芽孢杆菌糖化型α-淀粉酶的反应机制
J Biochem. 1977 Aug;82(2):417-27.
3
Tryptophan residues of saccharifying alpha-amylase from Bacillus subtilis. A kinetic discrimination of states of tryptophan residues using N-bromosuccinimide.枯草芽孢杆菌糖化α-淀粉酶的色氨酸残基。使用N-溴代琥珀酰亚胺对色氨酸残基状态进行动力学区分。
J Biochem. 1978 May;83(5):1503-10. doi: 10.1093/oxfordjournals.jbchem.a132060.
4
Substrate concentration dependence of the rate of maltose hydrolysis by saccharifying alpha-amylase from B. subtilis.枯草芽孢杆菌糖化型α-淀粉酶催化麦芽糖水解速率对底物浓度的依赖性
J Biochem. 1975 May;77(5):965-8. doi: 10.1093/oxfordjournals.jbchem.a130821.
5
Allosteric behavior irrespective of conformational change of enzyme protein. Sigmoidal concentration dependence of rate of action of saccharifying alpha-amylase on maltose.别构行为与酶蛋白的构象变化无关。糖化α-淀粉酶作用速率对麦芽糖的浓度依赖性呈S形。
FEBS Lett. 1976 Dec 31;72(2):283-6. doi: 10.1016/0014-5793(76)80987-8.
6
Kinetics and mechanism of transfer action of saccharifying alpha-amylase of Bacillus subtilis. Maltose--phenyl alpha-glucoside system.枯草芽孢杆菌糖化α-淀粉酶转糖基作用的动力学与机制。麦芽糖 - 苯基α-葡萄糖苷体系
J Biochem. 1969 Aug;66(2):183-90. doi: 10.1093/oxfordjournals.jbchem.a129134.
7
Hydrolysis of phenyl beta-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis.枯草芽孢杆菌糖化型α-淀粉酶催化苯基β-麦芽糖苷的水解反应
J Biochem. 1977 May;81(5):1187-92.
8
Quantitative determination of anomeric forms of sugar produced by amylases. V. Anomeric forms of maltose produced in the hydrolytic reaction of substituted phenyl alpha-maltosides catalyzed by saccharifying alpha-amylase from B. subtilis.淀粉酶产生的糖的异头物形式的定量测定。V. 枯草芽孢杆菌糖化α-淀粉酶催化的取代苯基α-麦芽糖苷水解反应中产生的麦芽糖的异头物形式。
J Biochem. 1975 Jun;77(6):1215-22.
9
Elucidation of the subsite structure of bacterial saccharifying alpha-amylase and its mode of degradation of maltose.细菌糖化α-淀粉酶亚位点结构及其对麦芽糖降解模式的阐释。
Carbohydr Res. 1996 Feb 28;282(1):171-80. doi: 10.1016/0008-6215(95)00365-7.
10
Kinetics and mechanism of hydrolysis of phenyl alpha-maltoside by saccharifying alpha-amylase of Bacillus subtilis. I. Formation of maltotriose in the course of hydrolysis.枯草芽孢杆菌糖化α-淀粉酶催化水解苯基α-麦芽糖苷的动力学及机制。I. 水解过程中麦芽三糖的形成
J Biochem. 1967 Oct;62(4):439-46. doi: 10.1093/oxfordjournals.jbchem.a128687.

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