74173-31-2

Basic information

• Product Name: 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE
• Synonyms: 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE;4-NITROPHENYL-ALPHA-D-MALTOHEPTOSIDE;PG7;P-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE;PNP-ALPHA-D-MALTOHEPTAOSIDE;p-Nitrophenyl-a-D-maltoheptaoside;alpha-d-Glucopyranoside, 4-nitrophenyl O-alpha-d-glucopyranosyl-(1->4)-O-alpha-d-glucopyranosyl-(1->4)-O-alpha-d-glucopyranosyl-(1->4)-O-alpha-d-glucopyranosyl-(1->4)-O-alpha-d-glucopyranosyl-(1->4)-O-alpha-d-glucopyranosyl-(1->4)-;4-Nitrophenyla-D-maltoheptaoside
• CAS NO: 74173-31-2
• Molecular Formula: C₄₈H₇₅NO₃₈
• Molecular Weight: 1274.09
• EINECS: 277-741-3
• Mol File: 74173-31-2.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 1498.2 °C at 760 mmHg
• Flash Point: 859.9 °C
• Appearance: /
• Density: 1.85 g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.714
• Storage Temp.: Store at 0°C
• PKA: 12.43±0.70(Predicted)
• CAS DataBase Reference: 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE(74173-31-2)
• EPA Substance Registry System: 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE(74173-31-2)

Safety Data

• Hazardous Substances Data: 74173-31-2(Hazardous Substances Data)

Usage

Description

4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is a chemical compound derived from alpha-D-maltoheptaoside, a carbohydrate. It serves as an artificial substrate in biochemical assays for studying enzyme activity, particularly glycosidases involved in carbohydrate metabolism. Its nitrophenyl group allows for colorimetric detection methods, making it valuable for research in biochemistry and the exploration of carbohydrate-modifying enzyme kinetics and mechanisms.

Uses

Used in Biochemical Research:
4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is used as a substrate in biochemical assays for studying the activity of enzymes, specifically glycosidases, which break down complex carbohydrates.
Used in Enzyme Activity Detection:
4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is used as a colorimetric detection agent in assays to identify and measure the activity of glycosidases, providing a visual indication of enzyme presence and function.
Used in Kinetics and Mechanism Studies:
4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is used as a research tool to explore the kinetics and mechanisms of carbohydrate-modifying enzymes, contributing to a deeper understanding of enzymatic processes in biochemistry.

InChI:InChI=1/C48H75NO38/c50-5-14-21(57)22(58)29(65)43(75-14)82-37-16(7-52)77-45(31(67)24(37)60)84-39-18(9-54)79-47(33(69)26(39)62)86-41-20(11-56)81-48(35(71)28(41)64)87-40-19(10-55)80-46(34(70)27(40)63)85-38-17(8-53)78-44(32(68)25(38)61)83-36-15(6-51)76-42(30(66)23(36)59)74-13-3-1-12(2-4-13)49(72)73/h1-4,14-48,50-71H,5-11H2/t14-,15-,16-,17-,18-,19-,20-,21-,22+,23-,24-,25-,26-,27-,28-,29-,30-,31-,32-,33-,34-,35-,36-,37-,38-,39-,40-,41-,42+,43-,44-,45-,46-,47-,48-/m1/s1

Upstream product

• 1184-46-9 D-maltohexaose 
• 3767-28-0 4-nitrophenyl-α-D-glucopyranoside 

Downstream Products

• 3482-57-3 p-nitrophenyl-α-D-glucopyranosyl-(1→4)-O-α-D-glucopyranoside 
• 100-02-7 4-nitro-phenol 
• 3767-28-0 4-nitrophenyl-α-D-glucopyranoside 

Relevant articles and documents

Enzymatic synthesis of p-nitrophenyl alpha-maltoheptaoside by transglycosylation of maltohexaose-forming amylase.

An extracellular maltohexaose-forming amylase [EC 3.2.1.98] from Klebsiella pneumoniae mutant is a normal hydrolytic enzyme that hydrolyzes short-chain amylose (DP = 23) to give about 40% maltohexaose. Transglycosylation from maltoheptaose to the 4-position of p-nitrophenyl alpha-glucoside was efficiently induced through the use of maltohexaose-forming amylase in an aqueous methanol solution. The enzyme specifically produced p-nitrophenyl alpha-maltoheptaoside (13% of the p-nitrophenyl alpha-glucoside) from maltoheptaose as a donor and p-nitrophenyl alpha-glucoside as an acceptor. The yield of p-nitrophenyl alpha-maltoheptaoside depended on the concentration of methanol solvent, the pH, and temperature. Furthermore, the use of the aqueous methanol system in the reaction not only improved the solubility of p-nitrophenyl alpha-glucoside but also greatly increased the formation of p-nitrophenyl alpha-maltoheptaoside, which is a useful substrate for assay of human amylase in serum and urine.