Comparison of the domain-level organization of starch hydrolases and related enzymes.
Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (beta/alpha)8-barrel and a smaller C-terminal domain as seen in crystal structures of alpha-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-alpha-1,6 linkages contain domains N-terminal to the (beta/alpha)8-barrel.
Jespersen
H M
HM
Department of Chemistry, Carlsberg Laboratory, Copenhagen Valby, Denmark.
MacGregor
E A
EA
Sierks
M R
MR
Svensson
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001236:Aspergillus oryzae / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology; D005959:Glucosidases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D013025:Glycine max / Q000201:enzymology; D013213:Starch / Q000378:metabolism*; D013552:Swine; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics
D013213:Starch; D005959:Glucosidases; D000516:alpha-Amylases