Study of the inhibition of four alpha amylases by acarbose and its 4IV-α-maltohexaosyl and 4IV-α-maltododecaosyl analogues

Yoon, Seung-Heon; Robyt, John F.

doi:10.1016/s0008-6215(03)00293-3

Cited by 72 publications

(50 citation statements)

References 33 publications

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“…For several enzymes of that family, it is a strong inhibitor, with inhibition constants in the M range (29,30,40,62). The reduced sensitivity of PyAMase to inhibition by acarbose compared to that of TtAMase is remarkable, which suggests that there are structural differences in the active sites of the two enzymes.…”

Section: Discussionmentioning

confidence: 99%

Amylomaltase ofPyrobaculum aerophilumIM2 Produces Thermoreversible Starch Gels

Kaper

Talik

Ettema

et al. 2005

Appl Environ Microbiol

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Amylomaltases are 4-␣-glucanotransferases (EC 2.4.1.25) of glycoside hydrolase family 77 that transfer ␣-1,4-linked glucans to another acceptor, which can be the 4-OH group of an ␣-1,4-linked glucan or glucose. The amylomaltase-encoding gene (PAE1209) from the hyperthermophilic archaeon Pyrobaculum aerophilum IM2 was cloned and expressed in Escherichia coli, and the gene product (PyAMase) was characterized. PyAMase displays optimal activity at pH 6.7 and 95°C and is the most thermostable amylomaltase described to date. The thermostability of PyAMase was reduced in the presence of 2 mM dithiothreitol, which agreed with the identification of two possible cysteine disulfide bridges in a three-dimensional model of PyAMase. The kinetics for the disproportionation of malto-oligosaccharides, inhibition by acarbose, and binding mode of the substrates in the active site were determined. Acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties. This thermoreversible gel has potential applications in the food industry. This is the first report on an archaeal amylomaltase.

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Section: Discussionmentioning

confidence: 99%

Amylomaltase ofPyrobaculum aerophilumIM2 Produces Thermoreversible Starch Gels

Kaper

Talik

Ettema

et al. 2005

Appl Environ Microbiol

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“…fermentation, consisting of a polyhydroxylated aminocyclohexene derivative (valienamine) linked via its nitrogen atom to a 6-deoxyglucose, which is itself α-1,4-linked to a maltose moiety. It is a competitive inhibitor of -amylase and the mechanism of inhibition seems to be due to the unsaturated cyclohexene ring and the glycosidic nitrogen linkage that mimics the transition state for the cleavage enzymatic of glycosidic linkages (42,43).…”

Section: Phytoconstituents With -Amylase Inhibitory Activitymentioning

confidence: 99%

α-Amylase Inhibitors: A Review of Raw Material and Isolated Compounds from Plant Source

et al. 2012

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-Inhibition of α-amylase, enzyme that plays a role in digestion of starch and glycogen, is considered a strategy for the treatment of disorders in carbohydrate uptake, such as diabetes and obesity, as well as, dental caries and periodontal diseases. Plants are an important source of chemical constituents with potential for inhibition of α-amylase and can be used as therapeutic or functional food sources. A review about crude extracts and isolated compounds from plant source that have been tested for α-amylase inhibitory activity has been done. The analysis of the results shows a variety of crude extracts that present α-amylase inhibitory activity and some of them had relevant activity when compared with controls used in the studies. Amongst the phyto-constituents that have been investigated, flavonoids are one of them that demonstrated the highest inhibitory activities with the potential of inhibition related to number of hydroxyl groups in the molecule of the compound. Several phyto-constituents and plant species as α-amylase inhibitors are being reported in this article. Majority of studies have focused on the anti-amylase phenolic compounds.

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“…Therefore, an ␣-glucosidase inhibitor extended on the reducing and/or nonreducing end by a malto-oligosaccharide so as to occupy the other subsites should make a good inhibitor of ␣-amylases. In the past, the main difficulty in testing this hypothesis has been in the synthesis of such extended ␣-glucosidase inhibitors, although some work to this end has been carried out (25)(26)(27)(28).…”

mentioning

confidence: 99%

In Situ Extension as an Approach for Identifying Novel α-Amylase Inhibitors

Numao

Damager

Li³

et al. 2004

Journal of Biological Chemistry

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A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of ␣-amylases based upon autoglucosylation of known ␣-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known ␣-glucosidase inhibitor, D-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic ␣-amylase with a K i value of 18 mM to a trisaccharide analogue with a K i value of 25 M. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any ␣-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.

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Study of the inhibition of four alpha amylases by acarbose and its 4IV-α-maltohexaosyl and 4IV-α-maltododecaosyl analogues

Cited by 72 publications

References 33 publications

Amylomaltase ofPyrobaculum aerophilumIM2 Produces Thermoreversible Starch Gels

Amylomaltase ofPyrobaculum aerophilumIM2 Produces Thermoreversible Starch Gels

α-Amylase Inhibitors: A Review of Raw Material and Isolated Compounds from Plant Source

In Situ Extension as an Approach for Identifying Novel α-Amylase Inhibitors

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