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Literature summary for 3.2.1.14 extracted from

  • Oku, T.; Ishikawa, K.
    Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: activity toward crystalline chitin (2006), Biosci. Biotechnol. Biochem., 70, 1696-1701.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
detection of two adjacent genes (PF1233 and PF1234) homologous to chitinase genes of Thermococcus kodakarensis in pyrococcus furiosus. In the cultured medium of Pyrococcus furiosus no chitinase is detected. On analysis of the structural gene of Pyrococcus furiosus, it appears that one nucleotide insertion in PF1234 causes a frame shift and separates a gene. By deletion of one nucleotide in PF1234, the best match is achieved between chitinases of Thermococcus kodakarensis and Pyrococcus furiosus. An artificial recombinant chitinase is constructed, exhibiting hydrolytic activity towards colloidal and crystalline chitins at high temperatures. Expression in Escherichia coli Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
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Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitin + H2O recombinant enzyme hydrolyzes colloidal and crystalline chitins Pyrococcus furiosus ?
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additional information chitinase is not important for the growth of Pyrococcus furiosus Pyrococcus furiosus ?
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