74173-31-2 Usage
General Description
4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is a chemical compound that is a derivative of alpha-D-maltoheptaoside, a type of carbohydrate. It is an artificial substrate used in biochemical assays to study the activity of enzymes, particularly those involved in carbohydrate metabolism. 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is often used in the study of glycosidases, which are enzymes that break down complex carbohydrates. Its nitrophenyl group makes it useful for colorimetric detection methods. 4-NITROPHENYL-ALPHA-D-MALTOHEPTAOSIDE is valuable for research in biochemistry and is utilized to explore the kinetics and mechanisms of carbohydrate-modifying enzymes.
Check Digit Verification of cas no
The CAS Registry Mumber 74173-31-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,4,1,7 and 3 respectively; the second part has 2 digits, 3 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 74173-31:
(7*7)+(6*4)+(5*1)+(4*7)+(3*3)+(2*3)+(1*1)=122
122 % 10 = 2
So 74173-31-2 is a valid CAS Registry Number.
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
74173-31-2Relevant articles and documents
Enzymatic synthesis of p-nitrophenyl alpha-maltoheptaoside by transglycosylation of maltohexaose-forming amylase.
Ogawa,Uejima,Nakakuki,Usui,Kainuma
, p. 581 - 586 (1990)
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.