Detail of "1492-30-4"

Reference

A macrocyclic enzyme model system

A macrocyclic enzyme model system. An electrostatic-hydrophobic double-field catalysis by a [20]paracyclophane in the deacylation of p-nitrophenyl hexadecanoate. Murakami, Yukito; Aoyama, Yasuhiro; Dobashi, Kazuyuki; Kida, Masaaki (Fac. Eng., Kyushu Univ., Fukuoka, Japan). Bull. Chem. Soc. Jpn., 49(12), 3633-6 (English) 1976. CODEN: BCSJA8. DOCUMENT TYPE: Journal CA Section: 22 (Physical Organic Chemistry) Section cross-reference(s): 7, 67 The catalytic functions of [(10-oxo-[20]paracyclophan-22(23)-yl)methyl]trimethylammonium chloride (I) in the hydrolysis and aminolysis reactions of p-nitrophenyl hexadecanoate (II) were investigated in 1% (v/v) methanol-1%(v/v)dioxane-water over the pH 9-10 region at 40.0.degree. and .mu. 1492-30-4 and 62248-80-0 which are cas registry numbers are also used here. = 0.2 (NaCl) with the initial II concn. 1.00 .times. 10-5 M. The paracyclophane (0.88 .times. 10-5 M) accelerated the hydrolysis of II by one order of magnitude at pH 9.7. The presence of either ethanolamine or glycine in the I-catalyzed deacylation of II resulted in further rate enhancement. The rate enhancement was brought about by the aminolysis reaction of II with the amines as confirmed by the product anal. The greater reactivity of glycine relative to that of ethanolamine was attributed to the electrostatic interactin between the anionic carboxylate group of glycine and the cationic ammonium group of I. The novel electrostatic-hydrophobic double-field catalyst was discussed for the glycinolysis reaction. .

Catalysis of reaction in organic solvent by enzyme displayed on the yeast cell surface as agglutinin fusion protein

Catalysis of reaction in organic solvent by enzyme displayed on the yeast cell surface as agglutinin fusion protein. Kawakami, Masayuki; Ueda, Atsumi; Nishigaki, Junji (Fuji Photo Film Co., Ltd., Japan). Jpn. 71-41-0 and 1492-30-4 are also occured in this study. Kokai Tokkyo Koho JP 2004049074 A2 19 Feb 2004, 13 pp. (Japanese). (Japan). CODEN: JKXXAF. CLASS: ICM: C12N015-09. ICS: C12N001-19; C12N009-00. APPLICATION: JP 2002-209316 18 Jul 2002. DOCUMENT TYPE: Patent CA Section: 7 (Enzymes) A method for carrying out an enzyme-catalyzed reaction in org. solvent or bilayer system of org. solvent and water using yeast expressing fusion protein of the enzyme with agglutinin on the cell surface, is disclosed. A Saccharomyces cerevisiae strain displaying an active lipase on the cell surface was constructed by cell surface engineering. The gene encoding Rhizopus oryzae lipase (ROL) was fused with the genes encoding the pre-a-factor leader sequence and the C-terminal half of a-agglutinin including the glycosylphosphatidylinositol-anchor attachment signal. The constructed gene was overexpressed under the control of the glyceraldehyde 3-phosphate dehydrogenase promoter. Linker peptides (spacers) consisting of the Gly/Ser repeat sequence were inserted at the C-terminal portion of ROL to enhance lipase activity by preserving the conformation of the active site near the C-terminal portion. Localization of the expressed ROL on the cell surface was confirmed by immunofluorescence microscopy. The rate of p-nitrophenyl palmitate (pNPP) hydrolysis in n-heptane by a lipase-a-agglutinin fusion protein prepn. was studied. Compared to Amano F-AP15, a dried powder of Rhizopus oryzae cell ext. contg. lipase, pNPP hydrolysis by lipase-a-agglutinin fusion expressing yeast was 1/5 in water, but 15 times higher in heptane. Esterification of palmitate and n-pentanol and of hardened oil with n-pentanol in heptane was also studied. In either case, lipase-a-agglutinin fusion expressing yeast provided a better catalysis compared to Amano F-AP15. .