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リコンビナント
expressed in E. coli
品質水準
フォーム
lyophilized powder
比活性
≥9 units/mg solid
分子量
90 kDa by SDS-PAGE
保管温度
−20°C
SMILES記法
OC(=O)CCCCCCCCCCCCC
InChI
1S/C14H28O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14(15)16/h2-13H2,1H3,(H,15,16)
InChI Key
TUNFSRHWOTWDNC-UHFFFAOYSA-N
関連するカテゴリー
詳細
Maltose phosphorylase (MP) is a dimeric enzyme. This enzyme is classified under family 65 of the glycoside hydrolases. It is a member of the disaccharide phosphorylase family.
アプリケーション
Maltose Phosphorylase from Enterococcus sp. has been used as a component in coupled assay and ATPase activity assay to study its effects on ATPase activity, on the 90 kDa heat shock proteins (Hsp90) ATPase reaction and on background absorbance on the production of resorufin.
Maltose phosphorylase from Enterococcus has been used in a study to describe a new pathway for maltose utilization in lactic acid bacteria. It has also been used in a study to describe the transfer of glucosyl moiety of maltose to acceptors with alcoholic OH groups.
生物化学的／生理学的作用
Enzymatically converts maltose to D-Glucose.
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose.
Maltose phosphorylase not only transfers glucosyl moieties from maltose to other sugars but has been shown to also use phenolic compounds such as salicyl alcohol as acceptors.
単位の定義
1 unitは、pH 7.0、30°C、1分間で、マルトースから1.0 μmoleのD-グルコースを生成します。
その他情報
ラクト-スを含有します。
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
M8284-1000UN:
M8284-BULK:
M8284-250UN:
M8284-VAR:
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M P Egloff et al.
Structure (London, England : 1993), 9(8), 689-697 (2001-10-06)
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose without requiring any cofactors, such as pyridoxal phosphate. The enzyme is part of operons that are involved in maltose/malto-oligosaccharide metabolism.
U Nilsson et al.
Microbiology (Reading, England), 147(Pt 6), 1565-1573 (2001-06-08)
Maltose phosphorylase (MP) from Lactococcus lactis was purified and the corresponding gene was cloned and expressed in Escherichia coli. The isoelectric point of the pure enzyme was determined to be 7.0. According to zymogram analysis and SDS-PAGE, the native MP
M Tangney et al.
FEMS microbiology letters, 76(1-2), 191-196 (1992-10-01)
Extracts prepared from cultures of Bacillus subtilis, grown on maltose as the sole carbon source, lacked maltose phosphotransferase system activity. There was, however, evidence for a maltose phosphorylase activity, and such extracts also possessed both glucokinase and glucose phosphotransferase system
Hiroyuki Nakai et al.
Carbohydrate research, 345(8), 1061-1064 (2010-04-16)
Lactobacillus acidophilus NCFM maltose phosphorylase (LaMalP) of glycoside hydrolase family 65 catalysed enzymatic synthesis of alpha-(1-->4)-glucosidic disaccharides from maltose and five monosaccharides in a coupled phosphorolysis/reverse phosphorolysis one-pot reaction. Thus phosphorolysis of maltose to beta-glucose 1-phosphate circumvented addition of costly
Y Le Breton et al.
Journal of applied microbiology, 98(4), 806-813 (2005-03-09)
The aim of this research was to characterize the metabolic pathway for maltose utilization in Enterococcus faecalis. Screening a library of Enterococcus faecalis insertional mutants allowed the isolation of mutants affected in maltose utilization. Genetic analysis of the insertion loci
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