Identification of Pyrococcus furiosus amylopullulanase catalytic residues

Applied Microbiology and Biotechnology

Volumn 66, Issue 4, 2005, Pages 408-413

  Kang, S ^a,b   Vieille, C ^a   Zeikus, J G ^a  

^a Michigan State University   (United States)

^b Michigan State University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLYSIS; MUTAGENESIS; PHASE SEQUENCE INDICATORS; STARCH;

CATALYTIC NUCLEOPHILES; CATALYTIC RESIDUES; PYROCOCCUS FURIOSUS AMYLOPULLULANASE (PFAPU);

CATALYSIS;

AMYLOPULLULANASE; BACTERIAL ENZYME; PULLULAN; STARCH; UNCLASSIFIED DRUG;

ENZYME;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN FAMILY; PYROCOCCUS FURIOSUS; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CIRCULAR DICHROISM; DNA, ARCHAEAL; GENE EXPRESSION; GENES, ARCHAEAL; GLUCANS; GLYCOSIDE HYDROLASES; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PYROCOCCUS FURIOSUS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STARCH;

FELIS CATUS; PYROCOCCUS; PYROCOCCUS FURIOSUS;

EID: 12144255190     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1690-7     Document Type: Article

References (18)

1. Bernfeld P (1955) Amylases α and β. Methods Enzymol 1:149-158
2. Brown SH, Costantino HR, Kelly RM (1990) Characterization of amylolytic activities associated with the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl Environ Microbiol 56:1985-1991
3. Costantino HR, Brown SH, Kelly RM (1990) Purification and characterization of an α-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105-115°C. J Bacteriol 172:3654-3660
4. Dong G, Vieille C, Savchenko A, Zeikus JG (1997a) Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl Environ Microbiol 63:3569-3576
5. Dong G, Vieille C, Zeikus JG (1997b) Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl Environ Microbiol 63:3577-3584
6. Erra-Pujada M, Debeire P, Duchiron F, O'Donohue MJ (1999) The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J Bacteriol 181:3284-3287
7. Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, Mizuno H (1998) Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose. J Mol Biol 277:393-407
8. Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316:695-696
9. Imamura H, Fushinobu S, Jeon BS, Wakagi T, Matsuzawa H (2001) Identification of the catalytic residue of Thermococcus litoralis 4-α-glucanotransferase through mechanism-based labeling. Biochemistry 40:12400-12406
10. Imamura H, Fushinobu S, Yamamoto M, Kumasaka T, Jeon BS, Wakagi T, Matsuzawa H (2003) Crystal structures of 4-α-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor. J Biol Chem 278:19378-19386
11. Janecek S (1998) Sequence of archaeal Methanococcus jannaschii α-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor? Folia Microbiol 43:123-128
12. Laderman KA, Asaka K, Uemori T, Mukai H, Taguchi Y, Kato I, Anfinsen CB (1993a) α-Amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli. J Biol Chem 268:24402-24407
13. Laderman KA, Davis BR, Krutzsch HC, Lewis MS, Griko YV, Privalov PL, Anfinsen CB (1993b) The purification and characterization of an extremely thermostable α-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. J Biol Chem 268:24394-24401
14. MacGregor EA, Janecek S, Svensson B (2001) Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim Biophys Acta 1546:1-20
15. McCarter JD, Withers SG (1996) Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae α-glucosidase using 5-fluoro glycosyl fluorides. J Biol Chem 271:6889-6894
16. Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
17. Sogaard M, Kadziola A, Haser R, Svensson B (1993) Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley α-amylase 1. J Biol Chem 268:22480-22484
18. Vieille C, Zeikus JG (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43