2006
DOI: 10.1016/j.jmb.2006.02.056
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Structure of the Sulfolobus solfataricus α-Glucosidase: Implications for Domain Conservation and Substrate Recognition in GH31

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Cited by 127 publications
(131 citation statements)
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“…Catalytic nucleophile D320 and acid/ base D416 found in MalA are identical to D518 and D616 in human acid a-glucosidase. Residues D212, R400, D416 and H480, which were deduced to be substrate binding residues in MalA (Ernst et al 2006), are identical to residues D404, R600, D616 and H674 in human acid a-glucosidase, respectively.…”
Section: Acid A-glucosidase Protein In Cultured Fibroblastsmentioning
confidence: 94%
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“…Catalytic nucleophile D320 and acid/ base D416 found in MalA are identical to D518 and D616 in human acid a-glucosidase. Residues D212, R400, D416 and H480, which were deduced to be substrate binding residues in MalA (Ernst et al 2006), are identical to residues D404, R600, D616 and H674 in human acid a-glucosidase, respectively.…”
Section: Acid A-glucosidase Protein In Cultured Fibroblastsmentioning
confidence: 94%
“…As a template, a-glucosidase MalA from Sulfolobus solfataricus (SwissProt Entry Name: AGLU_SULSO, Accession number: O59645, PDB ID: 2G3N), which belongs to glycoside hydrolase family 31 (GH31) (Ernst et al 2006) was used. According to sequence alignment, a model of the human wild-type acid a-glucosidase composed of 452 amino acids (residues 344-795) was modeled based on the template MalA (residues 152-604).…”
Section: Western Blot Analysismentioning
confidence: 99%
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“…Earlier, we built a structural model of the catalytic domain and the surrounding region of human acid a-glucosidase by means of homology modeling using the structural information on a-glucosidase MalA from Sulfolobus solfataricus (PDB: 2G3N) 10 as a template, and examined the structural changes caused by pathogenic and nonpathogenic amino acid substitutions. 11 However, the investigations were restricted to a limited region of the enzyme protein because the amino acid sequence identity between the human acid a-glucosidase and the template was low.…”
Section: Introductionmentioning
confidence: 99%
“…2) are even more prominent examples of such subtle sequence adjustment. The aspartate near the C-terminus of b7 is: (i) in GH-H an invariant catalytic site residue [3][4][5][6][7][8][9][10][11]; and (ii) in GH31 an invariant and important residue [23][24][25]. Structurally, however, the two aspartates do not correspond to each other (Fig.…”
Section: Remote Sequence Homologiesmentioning
confidence: 99%