Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2

Hee Yeon Cho, Young Wan Kim, Tae Jip Kim, Hee Seob Lee, Do Yeon Kim, Jung Wan Kim, Yin Won Lee, Soo Bok Lee, Kwan Hwa Park

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14 Citations (Scopus)


An additional amylase besides the typical α-amylase was detected in the cytoplasm of Bacillus subtilis SUH4-2, an isolate from Korean soil. The corresponding gene encoded a maltogenic amylase, which hydrolyzed cyclodextrin or starch to maltose and glucose; pullulan to panose; acarbose to glucose and acarviosine-glucose. Maltogenic amylase of B. subtilis SUH4-2 transferred sugar molecules to form various branched oligosaccharides upon the hydrolysis of substrates. The enzyme existed in a monomer-dimer equilibrium with a molar ratio of 3:2 in 50 mM KH2PO4-NaOH buffer (pH 7.0). The maltogenic amylase is most likely to be associated with carbohydrate metabolism in the cytoplasm, since the nucleotide sequence of the gene was highly homologous to the yvdF gene of B. subtilis 168, which is located in a gene cluster involved in maltose/maltodextrin utilization. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)333-340
Number of pages8
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Issue number2
Publication statusPublished - 2000 May 23

Bibliographical note

Funding Information:
This study was supported by the Korea Science and Engineering Foundation (KoSEF) through a grant endowed to the Research Center for New Bio-Materials in Agriculture and by the Korean Research Foundation through Grant G00030 to Prof. J.W. Kim.

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology


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