Literature DB >> 2676600

Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila.

J H Zhou1, T Baba, T Takano, S Kobayashi, Y Arai.   

Abstract

The nucleotide sequence of the Pseudomonas saccharophila gene encoding maltotetraohydrolase (G4-forming amylase) has been determined. The coding region for the G4-forming amylase precursor contained 1653 nucleotides. The deduced precursor protein included an N-terminal 21-residue putative signal peptide; the deduced mature form of G4-forming amylase contains 530 amino acid residues with a calculated molecular mass of 57 740 Da. Sequence similarities between the G4-forming amylase and other amylolytic enzymes of species ranging from prokaryotes to eukaryotes are quite limited. However, three regions, which are involved in both the catalytic and substrate-binding sites of various amylolytic enzymes, are highly conserved in the G4-forming amylase of P. saccharophila.

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Year:  1989        PMID: 2676600     DOI: 10.1016/0014-5793(89)81056-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  6 in total

1.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1991-02-25       Impact factor: 16.971

2.  Comparison of the domain-level organization of starch hydrolases and related enzymes.

Authors:  H M Jespersen; E A MacGregor; M R Sierks; B Svensson
Journal:  Biochem J       Date:  1991-11-15       Impact factor: 3.857

3.  A classification of glycosyl hydrolases based on amino acid sequence similarities.

Authors:  B Henrissat
Journal:  Biochem J       Date:  1991-12-01       Impact factor: 3.857

4.  Characteristics of two forms of alpha-amylases and structural implication.

Authors:  K Ohdan; T Kuriki; H Kaneko; J Shimada; T Takada; Z Fujimoto; H Mizuno; S Okada
Journal:  Appl Environ Microbiol       Date:  1999-10       Impact factor: 4.792

5.  Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme.

Authors:  T Nanmori; M Nagai; Y Shimizu; R Shinke; B Mikami
Journal:  Appl Environ Microbiol       Date:  1993-02       Impact factor: 4.792

6.  Characterization of the starch-acting MaAmyB enzyme from Microbacterium aurum B8.A representing the novel subfamily GH13_42 with an unusual, multi-domain organization.

Authors:  Vincent Valk; Rachel M van der Kaaij; Lubbert Dijkhuizen
Journal:  Sci Rep       Date:  2016-11-03       Impact factor: 4.379

  6 in total

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