74173-31-2

Usage

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 academic research and scientific papers

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.