Matches in SemOpenAlex for { <https://semopenalex.org/work/W1579305860> ?p ?o ?g. }
Showing items 1 to 99 of
99
with 100 items per page.
- W1579305860 endingPage "170" @default.
- W1579305860 startingPage "163" @default.
- W1579305860 abstract "Abstract α-Amylases (α-1,4-glucan 4-glucanohydrolase, E.C.3.2.1.1.) catalyze the cleavage of α-1,4-glucosidic linkages of starch components, glycogen, and various oligosaccharides. Thermostable α-amylases from Bacillus species are of great industrial importance in the production of corn syrup or dextrose. Thermostable α-amylase from Bacillus licheniformis , a monomeric enzyme with molecular mass of 55,200 Da (483 amino acid residues), shows a remarkable heat stability: its optimum temperature is 90°C and only 10% of activity is lost after heat treatment at 90°C for 30 min. Thus this enzyme provides an attractive model for investigating the structural basis for thermostability of proteins. The three-dimensional structure of thermostable α-amylase from Bacillus licheniformis has been determined by the multiple isomorphous replacement method of X-ray crystallography. The structure has been refined to a crystallographic R-factor of 0.199 for 58,601 independent reflections with F o >2σ(F o ) between 8.0 and 1.7resolution, with excellent stereochemistry. The final model consists of 468 amino acid residues and 294 water molecules. Missing from the model are the segment between Trp182 and Asn192 and both the N- and C-termini. The polypeptide chain fold into three distinct domains. The first domain (domain A), consisting of 291 residues (from residue 3 to 103 and 207 to 396), forms a (β/α) 8 -barrel structure. The second domain (domain B), consisting of residues 104 to 206, is inserted between the third β-strand and the third α-helix of domain A. The third C-terminal domain (domain C), consisting of residues 397 to 482, folds into an eight-stranded antiparallel β-barrel." @default.
- W1579305860 created "2016-06-24" @default.
- W1579305860 creator A5048108993 @default.
- W1579305860 creator A5048116356 @default.
- W1579305860 creator A5060047552 @default.
- W1579305860 creator A5069513324 @default.
- W1579305860 date "1996-01-01" @default.
- W1579305860 modified "2023-09-23" @default.
- W1579305860 title "Crystal structure of Bacillus licheniformis α-Amylase at 1.7resolution" @default.
- W1579305860 cites W1851792052 @default.
- W1579305860 cites W1918349277 @default.
- W1579305860 cites W1925779720 @default.
- W1579305860 cites W1966302520 @default.
- W1579305860 cites W1986191025 @default.
- W1579305860 cites W1987308950 @default.
- W1579305860 cites W1996680929 @default.
- W1579305860 cites W1998869143 @default.
- W1579305860 cites W2000612047 @default.
- W1579305860 cites W2039664027 @default.
- W1579305860 cites W2042987185 @default.
- W1579305860 cites W2046319395 @default.
- W1579305860 cites W2052344553 @default.
- W1579305860 cites W2054624750 @default.
- W1579305860 cites W2060262553 @default.
- W1579305860 cites W2065870143 @default.
- W1579305860 cites W2101749711 @default.
- W1579305860 cites W2103115788 @default.
- W1579305860 cites W2176060924 @default.
- W1579305860 cites W3076039 @default.
- W1579305860 doi "https://doi.org/10.1016/s0921-0423(96)80367-4" @default.
- W1579305860 hasPublicationYear "1996" @default.
- W1579305860 type Work @default.
- W1579305860 sameAs 1579305860 @default.
- W1579305860 citedByCount "1" @default.
- W1579305860 countsByYear W15793058602019 @default.
- W1579305860 crossrefType "book-chapter" @default.
- W1579305860 hasAuthorship W1579305860A5048108993 @default.
- W1579305860 hasAuthorship W1579305860A5048116356 @default.
- W1579305860 hasAuthorship W1579305860A5060047552 @default.
- W1579305860 hasAuthorship W1579305860A5069513324 @default.
- W1579305860 hasConcept C166940927 @default.
- W1579305860 hasConcept C170835558 @default.
- W1579305860 hasConcept C178790620 @default.
- W1579305860 hasConcept C181199279 @default.
- W1579305860 hasConcept C185592680 @default.
- W1579305860 hasConcept C2776527165 @default.
- W1579305860 hasConcept C2777272437 @default.
- W1579305860 hasConcept C2781216036 @default.
- W1579305860 hasConcept C521977710 @default.
- W1579305860 hasConcept C523546767 @default.
- W1579305860 hasConcept C54355233 @default.
- W1579305860 hasConcept C55493867 @default.
- W1579305860 hasConcept C71240020 @default.
- W1579305860 hasConcept C8010536 @default.
- W1579305860 hasConcept C86803240 @default.
- W1579305860 hasConceptScore W1579305860C166940927 @default.
- W1579305860 hasConceptScore W1579305860C170835558 @default.
- W1579305860 hasConceptScore W1579305860C178790620 @default.
- W1579305860 hasConceptScore W1579305860C181199279 @default.
- W1579305860 hasConceptScore W1579305860C185592680 @default.
- W1579305860 hasConceptScore W1579305860C2776527165 @default.
- W1579305860 hasConceptScore W1579305860C2777272437 @default.
- W1579305860 hasConceptScore W1579305860C2781216036 @default.
- W1579305860 hasConceptScore W1579305860C521977710 @default.
- W1579305860 hasConceptScore W1579305860C523546767 @default.
- W1579305860 hasConceptScore W1579305860C54355233 @default.
- W1579305860 hasConceptScore W1579305860C55493867 @default.
- W1579305860 hasConceptScore W1579305860C71240020 @default.
- W1579305860 hasConceptScore W1579305860C8010536 @default.
- W1579305860 hasConceptScore W1579305860C86803240 @default.
- W1579305860 hasLocation W15793058601 @default.
- W1579305860 hasOpenAccess W1579305860 @default.
- W1579305860 hasPrimaryLocation W15793058601 @default.
- W1579305860 hasRelatedWork W1977709772 @default.
- W1579305860 hasRelatedWork W1987307655 @default.
- W1579305860 hasRelatedWork W2004904454 @default.
- W1579305860 hasRelatedWork W2032986070 @default.
- W1579305860 hasRelatedWork W2042881674 @default.
- W1579305860 hasRelatedWork W2054003243 @default.
- W1579305860 hasRelatedWork W2059173138 @default.
- W1579305860 hasRelatedWork W2070546626 @default.
- W1579305860 hasRelatedWork W2072642261 @default.
- W1579305860 hasRelatedWork W2086056666 @default.
- W1579305860 hasRelatedWork W2094519349 @default.
- W1579305860 hasRelatedWork W2103499539 @default.
- W1579305860 hasRelatedWork W2144707401 @default.
- W1579305860 hasRelatedWork W2160125855 @default.
- W1579305860 hasRelatedWork W2161579403 @default.
- W1579305860 hasRelatedWork W2306004890 @default.
- W1579305860 hasRelatedWork W2348873687 @default.
- W1579305860 hasRelatedWork W2976654508 @default.
- W1579305860 hasRelatedWork W3150239404 @default.
- W1579305860 hasRelatedWork W3136136895 @default.
- W1579305860 isParatext "false" @default.
- W1579305860 isRetracted "false" @default.
- W1579305860 magId "1579305860" @default.
- W1579305860 workType "book-chapter" @default.