34620-76-3
Chemical Structure
Maltopentaose
Synonym(s): Maltopentose
- CAS No.: 34620-76-3
- Formula:C30H52O26
- Molecular Weight:828.72
IUPAC Name: (2R,3R,4R,5R)-4-(((2R,3R,4R,5S,6R)-5-(((2R,3R,4R,5S,6R)-5-(((2R,3R,4R,5S,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-(((2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)tetrahydro-2H-pyran-2-yl)oxy)-3,4-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)-3,4-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)-2,3,5,6-tetrahydroxyhexanal
InChIKey: FJCUPROCOFFUSR-GMMZZHHDSA-N
SMILES: O[C@H]1[C@@H]([C@H](O[C@H](O[C@]([C@@H]2O)([H])[C@H](O[C@H](O[C@@]([C@H](O)CO)([H])[C@H](O)[C@@H](O)C=O)[C@@H]2O)CO)[C@@H]1O)CO)O[C@@]([C@@H]([C@@H](O)[C@@H]3O[C@@]([C@@H]([C@@H](O)[C@@H]4O)O)([H])O[C@@H]4CO)O)([H])O[C@@H]3CO
Biological Activity: Maltopentaose is the shortest chain oligosaccharide. Maltopentaose is a substrate for α-amylases. Maltopentaose can be classified as maltodextrin and is also used in a study to investigate glycation and phosphorylation of α-lactalbumin. Maltopentaose is used to study the inhibition kinetics of human pancreatic α-amylase by dehydrodieugenol B[1][2][3].
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Maltopentaose | 99.97% | Maltopentaose is the shortest chain oligosaccharide. Maltopentaose is a substrate for α-amylases. Maltopentaose can be classified as maltodextrin and is also used in a study to investigate glycation and phosphorylation of α-lactalbumin. Maltopentaose is used to study the inhibition kinetics of human pancreatic α-amylase by dehydrodieugenol B. | ||||||||||||||||||||
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Maltopentaose (Standard) | ≥98% | Maltopentaose (Standard) is the analytical standard of Maltopentaose. This product is intended for research and analytical applications. Maltopentaose is the shortest chain oligosaccharide that can be classified as maltodextrin and is also used in a study to investigate glycation and phosphorylation of α-lactalbumin. | ||||||||||||||||||||
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- [1]. Maltopentaose is the shortest chain oligosaccharide that can be classified as maltodextrin and is also used in a study to investigate glycation and phosphorylation of α-lactalbumin. [Content Brief]
- [2]. Koukiekolo R, et al. Mechanism of porcine pancreatic alpha-amylase inhibition of amylose and maltopentaose hydrolysis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose. Eur J Biochem. 1999 Oct 1;265(1):20-6. [Content Brief]
- [3]. Dandekar PD, et al. Insights into the Inhibition Mechanism of Human Pancreatic α-Amylase, a Type 2 Diabetes Target, by Dehydrodieugenol B Isolated from Ocimum tenuiflorum. ACS Omega. 2021 Jan 13;6(3):1780-1786. [Content Brief]
