𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Monte Carlo simulation of multiple attack mechanism of α-amylase

✍ Scribed by Hiroshi Nakatani

Publisher
Wiley (John Wiley & Sons)
Year
1998
Tongue
English
Weight
379 KB
Volume
39
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

Porcine pancreatic a-amylase (EC 3.2. I . I ) produces short maltooligosaccharides from a single enzyme-substrate complex without dissociation by multiple or repetitive attack. Multiple attack is caused by relative sliding ofthe enzyme along the product chain ofthe enzyme-product complex without dissociation to form another productive complex. The Monte Carlo method was applied to the multiple attack mechanism to predict product distribution from amylose and amylopectin molecules of arbitrary sizes. The position ofthe initial attack to make the enzymesubstrate complex and branched reaction paths from the enzyme-product complex were selected by random numbers and probabilities. A simulated product distribution ,from 100,000 samples of amylose of chain length greater than 80 agreed completely with experimental data at the early stage of hydrolysis ofarnylose of mean chain length 90. On the other hand, the sirnulatedproduct distribution from amylopectin agreed with experimental data ofpotato amylopeclin when the djective chain length of the A chain was 9. Since the mean chain length of the A chain ofpotato amylopectin is 15, it is possible that amylopectin is partially compact in solution, so that the enzyme can recognize and act only on the outer side ofthe A chain at the early stage of digestion. 0 I996 John Wiley & Sons. Inc.

📜 SIMILAR VOLUMES

Monte Carlo simulation of multiple attac
Monte Carlo simulation of multiple attack mechanism of β-amylase-catalyzed reaction
✍ Hiroshi Nakatani 📂 Article 📅 1997 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 118 KB 👁 1 views

b-Amylase (EC 3.2.1.2) produces maltose (dimer) from the nonreducing ends of a-1,4 glucosidic bonds of substrates like maltooligosaccharides, amylose, and amylopectin. The enzyme releases several maltose molecules from a single enzyme-substrate complex without dissociation by multiple or repetitive

Constant number Monte Carlo simulation o
Constant number Monte Carlo simulation of population balances with multiple growth mechanisms
✍ Samira Khalili; Yulan Lin; Antonios Armaou; Themis Matsoukas 📂 Article 📅 2010 🏛 American Institute of Chemical Engineers 🌐 English ⚖ 378 KB

## Abstract We present a complete simulation scheme for particulate processes based on the constant number Monte Carlo methodology. Specifically, the proposed scheme can be applied towards the solution of population balances that include nucleation, coagulation and surface deposition, coupled to ch

Monte Carlo simulation of 4-α-glucanotra
Monte Carlo simulation of 4-α-glucanotransferase reaction
✍ Hiroshi Nakatani 📂 Article 📅 1999 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 123 KB 👁 1 views

## 4-␣-Glucanotransferase (GTase, D-enzyme) catalyzes disproportionation between two short polymers of maltooligosaccharides linked by ␣-1,4-glucoside bonds. Using action modes of the potato GTase for the donor and acceptor substrates, the Monte Carlo method was applied to simulate the GTase reac

Sampling configurations in Monte Carlo s
Sampling configurations in Monte Carlo simulations for quantum mechanical studies of solvent effects
✍ Kaline Coutinho; M. J. De Oliveira; Sylvio Canuto 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 159 KB 👁 1 views

Discrete models obtained from computer simulation are in increase use to study solvent effects. The approach consists of generating supermolecular structures for quantum mechanical calculations. The properties of the solute are calculated as an ensemble average over configurations generated by the s

Tertiary structure prediction of the KIX
Tertiary structure prediction of the KIX domain of CBP using Monte Carlo simulations driven by restraints derived from multiple sequence alignments
✍ Angel R. Ortiz; Andrzej Kolinski; Jeffrey Skolnick 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 274 KB 👁 1 views

Using a recently developed protein folding algorithm, a prediction of the tertiary structure of the KIX domain of the CREB binding protein is described. The method incorporates predicted secondary and tertiary restraints derived from multiple sequence alignments in a reduced protein model whose conf

A pH-dependent variation in α-helix stru
A pH-dependent variation in α-helix structure of the S-peptide of ribonuclease A studied by Monte Carlo simulated annealing
✍ Takashi Nakazawa; Sumiko Ban; Yuka Okuda; Masato Masuya; Ayori Mitsutake; Yuko O 📂 Article 📅 2002 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 386 KB

## Abstract Low‐energy conformations of the S‐peptide fragment (20 amino acid residues long) of ribonuclease A were studied by Monte Carlo simulated annealing. The obtained lowest‐energy structures have α‐helices with different size and location, depending distinctively on the ionizing states of ac