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

被引：56
作者：
Cho, HY
Kim, YW
Kim, TJ
Lee, HS
Kim, DY
Kim, JW
Lee, YW
Lee, SB
Park, KH [1 ]
机构：
[1] Seoul Natl Univ, Res Ctr New Biomat Agr, Suwon 441744, South Korea
[2] Seoul Natl Univ, Dept Food Sci & Technol, Suwon 441744, South Korea
[3] Univ Inchon, Dept Biol, Inchon 402749, South Korea
[4] Seoul Natl Univ, Div Appl Biol & Chem, Suwon 441744, South Korea
[5] Konkuk Univ, Inst Agr & Life Sci, Seoul 143701, South Korea
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1478卷 / 02期
关键词：
maltogenic amylase; transglycosylation; homodimer; yvdF; Bacillus subtilis;
D O I：
10.1016/S0167-4838(00)00037-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
An additional amylase besides the typical alpha-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. (C) 2000 Elsevier Science B.V. All rights reserved.
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页码：333 / 340
页数：8
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