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Title: Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland

Abstract

The complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase (thioesterase II) from rat mammary gland is presented. Most of the sequence was derived by analysis of (/sup 14/C)-labelled peptide fragments produced by cleavage at methionyl, glutamyl, lysyl, arginyl, and tryptophanyl residues. A small section of the sequence was deduced from a previously analyzed cDNA clone. The protein consists of 260 residues and has a blocked amino-terminal methionine and calculated M/sub r/ of 29,212. The carboxy-terminal sequence, verified by Edman degradation of the carboxy-terminal cyanogen bromide fragment and carboxypeptidase Y digestion of the intact thioesterase II, terminates with a serine residue and lacks three additional residues predicted by the cDNA sequence. The native enzyme contains three cysteine residues but no disulfide bridges. The active site serine residue is located at position 101. The rat mammary gland thioesterase II exhibits approximately 40% homology with a thioesterase from mallard uropygial gland, the sequence of which was recently determined by cDNA analysis. Thus the two enzymes may share similar structural features and a common evolutionary origin. The location of the active site in these thioesterases differs from that of other serine active site esterases; indeed, the enzymes domore » not exhibit any significant homology with other serine esterases, suggesting that they may constitute a separate new family of serine active site enzymes.« less

Authors:
;
Publication Date:
Research Org.:
Children's Hospital, Oakland, CA
OSTI Identifier:
6470364
Resource Type:
Journal Article
Journal Name:
Biochemistry; (United States)
Additional Journal Information:
Journal Volume: 26:5
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ESTERASES; AMINO ACID SEQUENCE; LABELLED COMPOUNDS; BIOLOGICAL EVOLUTION; CARBON 14 COMPOUNDS; CYSTEINE; LIQUID COLUMN CHROMATOGRAPHY; MAMMARY GLANDS; RATS; RECOMBINANT DNA; AMINO ACIDS; ANIMALS; BODY; CARBOXYLIC ACIDS; CHROMATOGRAPHY; DNA; ENZYMES; GLANDS; HYDROLASES; MAMMALS; MOLECULAR STRUCTURE; NUCLEIC ACIDS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; ORGANS; RODENTS; SEPARATION PROCESSES; THIOLS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Randhawa, Z I, and Smith, S. Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland. United States: N. p., 1987. Web. doi:10.1021/bi00379a024.
Randhawa, Z I, & Smith, S. Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland. United States. doi:10.1021/bi00379a024.
Randhawa, Z I, and Smith, S. Tue . "Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland". United States. doi:10.1021/bi00379a024.
@article{osti_6470364,
title = {Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland},
author = {Randhawa, Z I and Smith, S},
abstractNote = {The complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase (thioesterase II) from rat mammary gland is presented. Most of the sequence was derived by analysis of (/sup 14/C)-labelled peptide fragments produced by cleavage at methionyl, glutamyl, lysyl, arginyl, and tryptophanyl residues. A small section of the sequence was deduced from a previously analyzed cDNA clone. The protein consists of 260 residues and has a blocked amino-terminal methionine and calculated M/sub r/ of 29,212. The carboxy-terminal sequence, verified by Edman degradation of the carboxy-terminal cyanogen bromide fragment and carboxypeptidase Y digestion of the intact thioesterase II, terminates with a serine residue and lacks three additional residues predicted by the cDNA sequence. The native enzyme contains three cysteine residues but no disulfide bridges. The active site serine residue is located at position 101. The rat mammary gland thioesterase II exhibits approximately 40% homology with a thioesterase from mallard uropygial gland, the sequence of which was recently determined by cDNA analysis. Thus the two enzymes may share similar structural features and a common evolutionary origin. The location of the active site in these thioesterases differs from that of other serine active site esterases; indeed, the enzymes do not exhibit any significant homology with other serine esterases, suggesting that they may constitute a separate new family of serine active site enzymes.},
doi = {10.1021/bi00379a024},
journal = {Biochemistry; (United States)},
number = ,
volume = 26:5,
place = {United States},
year = {1987},
month = {3}
}