BBA - Proteins and Proteomics, 2004-02, Vol.1696 (2), p.165-170
2004
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Details
- Autor(en) / Beteiligte
- Titel
- The proteinaceous inhibitor of limit dextrinase in barley and malt
- Ist Teil von
- BBA - Proteins and Proteomics, 2004-02, Vol.1696 (2), p.165-170
- Ort / Verlag
- Netherlands: Elsevier B.V
- Erscheinungsjahr
- 2004
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Barley limit dextrinase catalyses hydrolysis of α-1,6- d-glucosidic bonds in branched poly- or oligosaccharides from starch. A specific inhibitor of this enzyme is found in mature barley kernels, but disappears after several days of germination. Two forms of this proteinaceous inhibitor, identical in amino acid sequence, have been isolated and characterized. They differ in attachment of cysteine or glutathione to a sulfhydryl group, possibly that of cysteine residue 59 of the inhibitor. They can form a 1:1 complex with limit dextrinase and are believed to interact specifically with the enzyme active site. The inhibitor present in mature barley can effectively reduce enzyme activity in barley germinated for a short time and in commercial malt.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1570-9639, 0006-3002eISSN: 1878-1454DOI: 10.1016/j.bbapap.2003.09.018Titel-ID: cdi_crossref_primary_10_1016_j_bbapap_2003_09_018
- Format
- –
- Schlagworte
- Barley, Complex formation, Edible Grain - metabolism, Enzyme Inhibitors - chemistry, Enzyme Inhibitors - isolation & purification, Enzyme Inhibitors - metabolism, Food-Processing Industry, Germination, Glycoside Hydrolases - antagonists & inhibitors, Hordeum - metabolism, Inhibitor specificity, Limit dextrinase, Limit dextrinase inhibitor, Models, Molecular, Plant Proteins - chemistry, Plant Proteins - isolation & purification, Plant Proteins - metabolism, Protein Isoforms - metabolism