Sökning: WFRF:(Allan P.)
> (1993-1994) >
Lipases from Rhizom...
Lipases from Rhizomucor miehei and Humicola lanuginosa : Modification of the lid covering the active site alters enantioselectivity
-
- Holmquist, Mats Torsten (författare)
- KTH,Biokemi och biokemisk teknologi
-
- Martinelle, Mats (författare)
- KTH,Industriell bioteknologi
-
- Berglund, P. (författare)
- Mid Sweden University
-
visa fler...
-
- Clausen, Ib Groth (författare)
- Novo-Nordisk A/S, Bagsvaerd, Denmark
-
Patkar, Shamkant (författare)
-
- Svendsen, Allan (författare)
- Novo-Nordisk A/S, Bagsvaerd, Denmark
-
- Hult, Karl (författare)
- KTH,Biokemi och biokemisk teknologi
-
visa färre...
-
(creator_code:org_t)
- 1993
- 1993
- Engelska.
-
Ingår i: Journal of Protein Chemistry. - 0277-8033. ; 12:6, s. 749-757
- Relaterad länk:
-
http://www.scopus.co...
-
visa fler...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- The homologous lipases from Rhizomucor miehei and Humicola lanuginosa showed approximately the same enantioselectivity when 2-methyldecanoic acid esters were used as substrates. Both lipases preferentially hydrolyzed the S- enantiomer of 1-heptyl 2-methyldecanoate (R. miehei: E(S) = 8.5; H. lanuginosa: E(S) = 10.5), but the R-enantiomer of phenyl 2-methyldecanoate (E(R) = 2.9). Chemical arginine specific modification of the R. miehei lipase with 1,2-cyclohexanedione resulted in a decreased enantioselectivity (E(R) = 2.0), only when the phenyl ester was used as a substrate. In contrast, treatment with phenylglyoxal showed a decreased enantioselectivity (E(S) = 2.5) only when the heptyl ester was used as a substrate. The presence of guanidine, an arginine side chain analog, decreased the enantioselectivity with the heptyl ester (E(S) = 1.9) and increased the enantioselectivity with the aromatic ester (E(R) = 4.4) as substrates. The mutation, Glu 87 Ala, in the lid of the H. lanuginosa lipase, which might decrease the electrostatic stabilization of the open-lid conformation of the lipase, resulted in 47% activity compared to the native lipase, in a tributyrin assay. The Glu 87 Ala mutant showed an increased enantioselectivity with the heptyl ester (E(S) = 17.4) and a decreased enantioselectivity with the phenyl ester (E(R) = 2.5) as substrates, compared to native lipase. The enantioselectivities of both lipases in the esterification of 2-methyldecanoic acid with 1-heptanol were unaffected by the lid modifications.
Ämnesord
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
Nyckelord
- alanine
- arginine
- decanoic acid derivative
- ester
- guanidine
- heptanol
- phenylglyoxal
- triacylglycerol lipase
- article
- chemical modification
- enantiomer
- enzyme activation
- enzyme active site
- enzyme conformation
- enzyme substrate
- esterification
- gas chromatography
- hydrolysis
- lipid metabolism
- nonhuman
- site directed mutagenesis
- Comparative Study
- Cyclohexanones
- Decanoates
- Enzymes
- Immobilized
- Kinetics
- Lipase
- Mitosporic Fungi
- Mucorales
- Stereoisomerism
- Substrate Specificity
- Support
- Non-U.S. Gov't
- Humicola
- Rhizomucor miehei
- Thermomyces lanuginosus
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas