53298
Methyl 4-methylumbelliferyl hexylphosphonate
≥95.0% (HPLC)
别名:
Hexylphosphonic acid methyl 4-methylumbelliferyl ester
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关于此项目
经验公式（希尔记法）:
C17H23O5P
化学文摘社编号:
分子量:
338.34
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.77
SMILES string
O=P(OC)(CCCCCC)OC1=CC=C(C(C)=CC(O2)=O)C2=C1
InChI
1S/C17H23O5P/c1-4-5-6-7-10-23(19,20-3)22-14-8-9-15-13(2)11-17(18)21-16(15)12-14/h8-9,11-12H,4-7,10H2,1-3H3
InChI key
UDTZADITECBVLJ-UHFFFAOYSA-N
assay
≥95.0% (HPLC)
storage temp.
−20°C
Application
This lipase suicide inhibitor can be utilized to determine lipase and hydrolase activity, even in complex protein mixtures. The molar amount of enzyme can be determined by active site titration experiments. This inhibitor is soluble in both DMF and DMSO. Active site titrations should be performed in a pH range from 7-8 considering that higher pH values can lead to appreciable spontaneous hydrolysis. It is recommended to perform corresponding negative controls (buffer only).
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Zhen Qian et al.
Chembiochem : a European journal of chemical biology, 8(16), 1989-1996 (2007-09-19)
The engineering of lipase B from Candida antarctica (CALB) by circular permutation has yielded over sixty hydrolase variants, and several show significantly improved catalytic performance. Here we report a detailed characterization of ten selected enzyme variants by kinetic and spectroscopic
Zi Jin et al.
Analytical biochemistry, 450, 46-48 (2014-01-11)
We describe a method for quantification of displayed lipase on yeast cell surface. The strategy uses an organophosphonate ester to irreversibly inhibit the active lipase and release a detectable fluorescent group. The amount of displayed lipase can be represented as
Anders O Magnusson et al.
Chembiochem : a European journal of chemical biology, 6(6), 1051-1056 (2005-05-11)
The active site of Candida antarctica lipase B (CALB) hosts the catalytic triad (Ser-His-Asp), an oxyanion hole and a stereospecificity pocket. During catalysis, the fast-reacting enantiomer of secondary alcohols places its medium-sized substituent in the stereospecificity pocket and its large
Lipase chemoselectivity towards alcohol and thiol acyl acceptors in a transacylation reaction
Hedfors, C., et al.
Journal of Molecular Catalysis. B, Enzymatic, 66, 120-123 (2010)
Active-site titration analysis of surface influences on immobilized Candida antarctica lipase B activity
Laszlo, J. A., et al.
Journal of Molecular Catalysis. B, Enzymatic, 69, 60-65 (2011)
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