Structural highlights
Function
SUSB_BACTN Glucoamylase that hydrolyzes alpha-1,4-glucosidic linkages, alpha-1,6-, alpha-1,3- and alpha-1,2-glucosidic linkages during starch degradation.[1] [2]
Publication Abstract from PubMed
The role of calcium ion in the active site of the inverting glycoside hydrolase family 97 enzyme, BtGH97a, was investigated through structural and kinetic studies. The calcium ion was likely directly involved in the catalytic reaction. The pH dependence of kcat/Km values in the presence or absence of calcium ion indicated that the calcium ion lowered the pKa of the base catalyst. The significant decreases in kcat/Km for hydrolysis of substrates with basic leaving groups in the absence of calcium ion confirmed that the calcium ion facilitated the leaving group departure.
Catalytic role of the calcium ion in GH97 inverting glycoside hydrolase.,Okuyama M, Yoshida T, Hondoh H, Mori H, Yao M, Kimura A FEBS Lett. 2014 Aug 25;588(17):3213-7. doi: 10.1016/j.febslet.2014.07.002. Epub , 2014 Jul 10. PMID:25017438[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ D'Elia JN, Salyers AA. Contribution of a neopullulanase, a pullulanase, and an alpha-glucosidase to growth of Bacteroides thetaiotaomicron on starch. J Bacteriol. 1996 Dec;178(24):7173-9. PMID:8955399
- ↑ Kitamura M, Okuyama M, Tanzawa F, Mori H, Kitago Y, Watanabe N, Kimura A, Tanaka I, Yao M. Structural and functional analysis of a glycoside hydrolase family 97 enzyme from Bacteroides thetaiotaomicron. J Biol Chem. 2008 Dec 26;283(52):36328-37. Epub 2008 Nov 3. PMID:18981178 doi:10.1074/jbc.M806115200
- ↑ Okuyama M, Yoshida T, Hondoh H, Mori H, Yao M, Kimura A. Catalytic role of the calcium ion in GH97 inverting glycoside hydrolase. FEBS Lett. 2014 Aug 25;588(17):3213-7. PMID:25017438 doi:10.1016/j.febslet.2014.07.002
