Literature DB >> 10452542

The evolution of starch-binding domain.

S Janecek1, J Sevcík.   

Abstract

Amylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain the starch-binding domain (SBD) positioned almost exclusively at the C-terminus. Detailed analysis of all available SBD sequences from 43 different amylases revealed its independent evolutionary behaviour with regard to the catalytic domains. In the evolutionary tree based on sequence alignment of the SBDs, taxonomy is respected so that fungi and actinomycetes form their own separate parts surrounded by bacteria that are also clustered according to taxonomy. The only known N-terminal SBD from Rhizopus oryzae glucoamylase is on the longest branch separated from all C-terminal SBDs. The 3-dimensional (3-D) structures of fungal glucoamylase and bacterial CGTase SBDs are compared and used to discuss the interesting SBD evolution.

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Year:  1999        PMID: 10452542     DOI: 10.1016/s0014-5793(99)00919-9

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


  23 in total

1.  Comparative characterization of complete and truncated forms of Lactobacillus amylovorus alpha-amylase and role of the C-terminal direct repeats in raw-starch binding.

Authors:  R Rodriguez Sanoja; J Morlon-Guyot; J Jore; J Pintado; N Juge; J P Guyot
Journal:  Appl Environ Microbiol       Date:  2000-08       Impact factor: 4.792

2.  Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain.

Authors:  Naeem Rashid; Joel Cornista; Satoshi Ezaki; Toshiaki Fukui; Haruyuki Atomi; Tadayuki Imanaka
Journal:  J Bacteriol       Date:  2002-02       Impact factor: 3.490

3.  Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains.

Authors:  D Guillén; M Santiago; L Linares; R Pérez; J Morlon; B Ruiz; S Sánchez; R Rodríguez-Sanoja
Journal:  Appl Environ Microbiol       Date:  2007-04-27       Impact factor: 4.792

Review 4.  Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.

Authors:  Matthew S Gentry; Carlos Romá-Mateo; Pascual Sanz
Journal:  FEBS J       Date:  2012-03-16       Impact factor: 5.542

Review 5.  α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.

Authors:  Štefan Janeček; Birte Svensson; E Ann MacGregor
Journal:  Cell Mol Life Sci       Date:  2013-06-27       Impact factor: 9.261

6.  Microbial starch-binding domains as a tool for targeting proteins to granules during starch biosynthesis.

Authors:  Qin Ji; Jean-Paul Vincken; Luc C J M Suurs; Richard G F Visser
Journal:  Plant Mol Biol       Date:  2003-03       Impact factor: 4.076

7.  Adhesion of bifidobacteria to granular starch and its implications in probiotic technologies.

Authors:  R Crittenden; A Laitila; P Forssell; J Mättö; M Saarela; T Mattila-Sandholm; P Myllärinen
Journal:  Appl Environ Microbiol       Date:  2001-08       Impact factor: 4.792

8.  The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding.

Authors:  Wei-I Chou; Tun-Wen Pai; Shi-Hwei Liu; Bor-Kai Hsiung; Margaret D-T Chang
Journal:  Biochem J       Date:  2006-06-15       Impact factor: 3.857

9.  Glucoamylase starch-binding domain of Aspergillus niger B1: molecular cloning and functional characterization.

Authors:  Tzur Paldi; Ilan Levy; Oded Shoseyov
Journal:  Biochem J       Date:  2003-06-15       Impact factor: 3.857

10.  Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism.

Authors:  Matthew S Gentry; Rachel M Pace
Journal:  BMC Evol Biol       Date:  2009-06-22       Impact factor: 3.260

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