The fully conserved Asp residue in conserved sequence region I of the α‐amylase family is crucial for the catalytic site architecture and activity
- 25 March 2003
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 541 (1-3), 47-51
- https://doi.org/10.1016/s0014-5793(03)00286-2
Abstract
The α‐amylase family is a large group of starch processing enzymes [Svensson, B. (1994) Plant Mol. Biol. 25, 141–157]. It is characterized by four short sequence motifs that contain the seven fully conserved amino acid residues in this family: two catalytic carboxylic acid residues and four substrate binding residues. The seventh conserved residue (Asp135) has no direct interactions with either substrates or products, but it is hydrogen‐bonded to Arg227, which does bind the substrate in the catalytic site. Using cyclodextrin glycosyltransferase as an example, this paper provides for the first time definite biochemical and structural evidence that Asp135 is required for the proper conformation of several catalytic site residues and therefore for activity.Keywords
This publication has 38 references indexed in Scilit:
- The Remote Substrate Binding Subsite −6 in Cyclodextrin-glycosyltransferase Controls the Transferase Activity of the Enzyme via an Induced-fit MechanismJournal of Biological Chemistry, 2002
- Crystal Structures of Amylosucrase from Neisseria polysaccharea in Complex with d-Glucose and the Active Site Mutant Glu328Gln in Complex with the Natural Substrate SucroseBiochemistry, 2001
- Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase α-cyclodextrin productionJournal of Molecular Biology, 2000
- Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolutionJournal of Molecular Biology, 1999
- Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolutionJournal of Molecular Biology, 1998
- The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 å resolution: structural characterization of proline-substitution sites for protein thermostabilizationJournal of Molecular Biology, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- Nucleotide Sequence and X-ray Structure of Cyclodextrin Glycosyltransferase from Bacillus circulans Strain 251 in a Maltose-dependent Crystal FormJournal of Molecular Biology, 1994
- The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping‐Pong mechanismFEBS Letters, 1994