Isolation, properties, and the complete amino acid sequence of a second form of 60-kDa glycoprotein esterase. Orientation of the 60-kDa proteins in the microsomal membrane.
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TLDR
Results, in addition to the finding of an N-linked carbohydrate, suggest that the two 60-kDa proteins are oriented on the luminal side of the endoplasmic membrane.About:
This article is published in Journal of Biological Chemistry.The article was published on 1989-07-25 and is currently open access. It has received 88 citations till now. The article focuses on the topics: Peptide sequence & Sequence analysis.read more
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Journal ArticleDOI
THE MAMMALIAN CARBOXYLESTERASES: From Molecules to Functions
Tetsuo Satoh,Masakiyo Hosokawa +1 more
TL;DR: A comparison of the nucleotide and amino acid sequence of the mammalian carboxylesterases shows that all forms expressed in the rat can be assigned to one of three gene subfamilies with structural identities of more than 70% within each subfamily.
Journal ArticleDOI
Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins
Miroslaw Cygler,Joseph D. Schrag,Joel L. Sussman,Michal Harel,Israel Silman,Mary K. Gentry,Bhupendra P. Doctor +6 more
TL;DR: An improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained, and 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved.
Journal ArticleDOI
Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents.
TL;DR: Although the contributions of individual effective amino acid substitutions to enhanced activity are small (<2-fold increases), the accumulation of multiple mutations by directed evolution allows significant improvement of the biocatalyst for reactions on substrates and under conditions not already optimized in nature.
Journal ArticleDOI
Structure, function and regulation of carboxylesterases.
TL;DR: A novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties is proposed to allay the confusion of the classic classification of car boxylesterase isozymes.
Journal ArticleDOI
Structure and Catalytic Properties of Carboxylesterase Isozymes Involved in Metabolic Activation of Prodrugs
TL;DR: Experimentation for an understanding of detailed substrate specificity of prodrugs for CES isozymes and its hydrolysates will help to design the ideal pro drugs.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal ArticleDOI
Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.
TL;DR: Small amounts of myoglobin, beta-lactoglobulin, and other proteins and peptides can be spotted or electroblotted onto polyvinylidene difluoride membranes, stained with Coomassie Blue, and sequenced directly, suggesting that PVDF membranes are superior supports for sequence analysis of picomole quantities of proteins purified by gel electrophoresis.
Journal ArticleDOI
Assembly of asparagine-linked oligosaccharides.
TL;DR: The structure of ASPARAGINE-LINKed OLIGOSACCI-IARIDES and transfer-Oligosaccharide Structural Requirements, and Sequence of Processing and Specificity of Processing Enzymes are presented.
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Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins.
TL;DR: The algorithm is shown to be at least as good as, and usually superior to, the reported prediction methods assessed in the same way and the implication in protein folding is discussed.
Journal ArticleDOI
A C-terminal signal prevents secretion of luminal ER proteins
Sean Munro,Hugh R.B. Pelham +1 more
TL;DR: It is proposed that the KDEL sequence marks proteins that are to be retained in the ER and discuss possible retention mechanisms.
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Complete covalent structure of 60-kDa esterase isolated from 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced rabbit liver microsomes.
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