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Open AccessJournal ArticleDOI

Catalytic properties of the cloned amylase from Bacillus licheniformis

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TLDR
The purified enzyme encoded by pIJ322 was capable of hydrolyzing pullulan and cyclodextrin as well as starch and degraded soluble starch by cleaving maltose units preferentially but did not attack alpha-1,6-linkage.
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This article is published in Journal of Biological Chemistry.The article was published on 1992-11-05 and is currently open access. It has received 105 citations till now. The article focuses on the topics: Bacillus licheniformis & Maltose.

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Properties and applications of starch-converting enzymes of the α-amylase family

TL;DR: The alpha-amylase family of glycosyl hydrolases as discussed by the authors is one of the most common types of enzymes used in industrial applications and has a (beta/alpha) 8-barrel structure with conserved amino acid residues.
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Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.

TL;DR: The sequence- Specificity and structure-specificity relationships described may provide useful pointers for rational protein engineering.
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The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.

TL;DR: From the further analysis of the genome sequence, conserved regulatory DNA motives, the occurrence of the glyoxylate bypass and the presence of anaerobic ribonucleotide reductase explaining that B. licheniformis is able to grow on acetate and 2,3-butanediol as well as anaerobically on glucose.
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Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.

TL;DR: Activity and specificity of the enzymes are discussed in terms of conserved amino acid residues and loop variations, and an evolutionary distance tree of 47 amylolytic and related enzymes is built on 37 residues representing the four best conserved β-strands of the barrel.
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Structure specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family

TL;DR: The present review discusses the multiple specificity in the light of the oligomerization and the molecular structures arriving at a clarified enzyme classification and a physiological role of the enzymes is proposed.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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Fate of transforming DNA following uptake by competent Bacillus subtilis. I. Formation and properties of the donor-recipient complex.

TL;DR: The recovery of donor transforming activity following eclipse, and the appearance of recombinant activity, previously reported by Venema, Pritchard & Venema-Schroder (1965) , is shown to be due to changes occurring in the donor—recipient complex.
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Complete nucleotide sequence of a gene coding for heat- and pH-stable alpha-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying alpha-amylases deduced from the DNA sequences.

TL;DR: The gene coding for the heat-stable and pH-stable alpha-amylase of Bacillus licheniformis 584 was cloned in Escherichia coli and the nucleotide sequence of a DNA fragment containing the entire amylase gene was determined.
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Paper ionophoresis of carbohydrates. I. Procedures and results for four electrolytes

TL;DR: In this article, a procedure for effecting paper ionophoresis of polyhydroxy compounds in the electrolytes borax, sodium arsenite, basic lead acetate, and sodium hydroxide is described.
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