Molecular cloning of endo-beta-D-1,4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae

J Bacteriol. 2003 Mar;185(5):1749-56. doi: 10.1128/JB.185.5.1749-1756.2003.

Abstract

Three endoglucanase genes, designated the rce1, rce2, and rce3 genes, were isolated from Rhizopus oryzae as the first cellulase genes from the subdivision ZYGOMYCOTA: All the amino acid sequences deduced from the rce1, rce2, and rce3 genes consisted of three distinct domains: cellulose binding domains, linker domains, and catalytic domains belonging to glycosyl hydrolase family 45. The rce3 gene had two tandem repeated sequences of cellulose binding domains, while rce1 and rce2 had only one. rce1, rce2, and rce3 had various lengths of linker sequences.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Catalytic Domain
  • Cellulase / chemistry
  • Cellulase / genetics*
  • Cellulase / metabolism*
  • Cloning, Molecular
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Glycosylation
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Rhizopus / genetics*
  • Saccharomyces cerevisiae / genetics
  • Sequence Homology, Amino Acid

Substances

  • Fungal Proteins
  • Recombinant Proteins
  • Cellulase

Associated data

  • GENBANK/AB047927
  • GENBANK/AB056668