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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

Substrate concentration dependence of the rate of maltose hydrolysis by saccharifying alpha-amylase from B. subtilis.

作者信息

Shibaoka T, Inatani T, Hiromi K, Watanabe T

出版信息

J Biochem. 1975 May;77(5):965-8. doi: 10.1093/oxfordjournals.jbchem.a130821.

DOI:10.1093/oxfordjournals.jbchem.a130821
PMID:808539
Abstract
  1. The action of saccharifying alpha-amylase from B. subtilis [EC 3.2.1.1] on eq- (the equilibrium mixture of alpha- and beta-forms) and beta-maltose was studied at pH 5.4 and 25 degrees. 2. The plots of initial velocity versus substrate concentration showed remarkable sigmoidal curves for both substrates. 3. The value of Hill's coefficient for eq- and beta-maltose were determined to be 3.3 and 3.8, respectively.
摘要
  1. 在pH 5.4和25摄氏度条件下，研究了枯草芽孢杆菌[EC 3.2.1.1]的糖化α-淀粉酶对α-和β-型平衡混合物（eq-）以及β-麦芽糖的作用。2. 初始速度与底物浓度的关系图显示，两种底物均呈现出明显的S形曲线。3. 确定eq-和β-麦芽糖的希尔系数分别为3.3和3.8。

相似文献

1
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.
2
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.
3
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.
4
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.
5
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.
6
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.
7
Kinetics and mechanism of hydrolysis of phenyl alpha-maltos- ide by saccharifying alpha-amylase of Bacillus subtilis. II. Dependence of the rates of formation of phenol, phenyl alpha-glucoside and maltotriose on the substrate concentration.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。II. 苯酚、苯基α-葡萄糖苷和麦芽三糖生成速率对底物浓度的依赖性。
J Biochem. 1969 May;65(5):741-50. doi: 10.1093/oxfordjournals.jbchem.a129072.
8
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.
9
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.
10
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.