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Thermoactinomyces vulgaris

Known as: Thermoactinomyces candidus 
 
National Institutes of Health

Related topics

Related topics

4 relations
Extrinsic allergic alveolitisMushroom Worker's LungSuberosisThermoactinomyces vulgaris antigen

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2005
2005
Complexes of Thermoactinomyces vulgaris R‐47 α‐amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α‐(1,6) glycosidic linkages
Thermoactinomyces vulgaris R‐47 α‐amylase 1 (TVAI) has unique hydrolyzing activities for pullulan with sequence repeats of α‐(1,4… Expand
2004
2004
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
Alphan alpha-amylase (TVA II) from Thermoactinomyces vulgaris R-47 efficiently hydrolyzes alpha-1,4-glucosidic linkages of… Expand
2001
2001
Novel glucoamylase-type enzymes from Thermoactinomyces vulgaris and Methanococcus jannaschii whose genes are found in the flanking region of the α-amylase genes
Abstract. A region downstream of the gene for pullulan-hydrolyzing α-amylase, TVA II, of Thermoactinomyces vulgaris R-47 was… Expand
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2000
2000
DNA-DNA relatedness among Thermoactinomyces species: Thermoactinomyces candidus as a synonym of Thermoactinomyces vulgaris and Thermoactinomyces thalpophilus as a synonym of Thermoactinomyces…
DNA-DNA relatedness of all validly described Thermoactinomyces species was determined to infer the genetic relationships between… Expand
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Highly Cited
1999
Highly Cited
1999
Isolation and partial characterisation of extracellular keratinase from a wool degrading thermophilic actinomycete strain Thermoactinomyces candidus.
The keratinase production by the thermophilic actinomycete strain Thermoactinomyces candidus was induced by sheep wool as the… Expand
Highly Cited
1995
Highly Cited
1995
Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing alpha-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47.
Thermoactinomyces vulgaris R-47 produces two alpha-amylases, TVA I, an extracellular enzyme, and TVA II, an intracellular enzyme… Expand
Highly Cited
1992
Highly Cited
1992
Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris.
The crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris has been determined at 0.235-nm resolution by X-ray… Expand
1991
1991
Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T A metalloenzyme endowed with dual substrate specificity
A gene coding for an extracellular Zn‐carboxypeptidase of Thermoactinomyces vulgaris has been cloned and sequenced (EMBL X56901… Expand
1988
1988
Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglin
Thermitase, the thermostable alkaline protease from Thermoactinomyces vulgaris, has been crystallised in a 1:1 complex with eglin… Expand
1981
1981
Influence of calcium binding on the thermal stability of 'thermitase', a serine protease from Thermoactinomyces vulgaris.
'Thermitase' (EC 3.4.21.14), a thermostable extracellular serine protease from Thermoactinomyces vulgaris, binds one calcium ion… Expand
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