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pubmed-article:122569pubmed:abstractText1. Using derivatives or non-symmetrical analogs of alpha,alpha-trehalose, we studied the catalytic specificities of trehalases from various species: Pseudomonas fluorescens, Melolontha vulgaris, porcine and human kidneys. 2. alpha,Beta-trehalose, beta,beta-trehalose, 6,6'dideoxy alpha,alpha-trehalose, alpha-D-xylopyranosyl alpha-D-xylopyranoside were shown to be neither substrates nor inhibitors. 3. 6'deoxy alpha,alpha-trehalose, alpha-D-glucopyranosyl alpha-D-xylopyranoside, alpha-D-allopyranosyl alpha-D-glucopyranoside and alpha-D-galactosyl alpha-D-glucopyranoside, which all possess an intact alpha-D-glucopyranosyl residue, were split by all these trehalases. 4. alpha-D-glucopyranosyl alpha-D-mannopyranoside, alpha,alpha-trehalosamine are competitive inhibitors. 5. These results show the importance of the primary alcohol group at C-6, of the equatorial configuration of the OH groups at C-2, C-3 and C-4 and of the modification of the structure at C-2 of the substrate for the catalytic activity.lld:pubmed
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pubmed-article:122569pubmed:pagination111-4lld:pubmed
pubmed-article:122569pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:122569pubmed:year1978lld:pubmed
pubmed-article:122569pubmed:articleTitleComparative specificities of trehalases from various species.lld:pubmed
pubmed-article:122569pubmed:affiliationLaboratoire de Chimie Biologique, E.R.A. No. 99 du C.N.R.S. Faculté des Sciences Pharmaceutiques et Biologiques, Paris, France.lld:pubmed
pubmed-article:122569pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:122569pubmed:publicationTypeComparative Studylld:pubmed
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