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Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis.
Phosphorylation of purified Na+,K(+)-ATPase by cAMP-dependent protein kinase (protein kinase A) decreases the activity of this enzyme. We have now shown, using several experimental approaches, that aExpand
Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase.
BACKGROUND Candida cylindracea cholesterol esterase (CE) reversibly hydrolyzes cholesteryl linoleate and oleate. CE belongs to the same alpha/beta hydrolase superfamily as triacylglycerol acylExpand
Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations.
The 500-residue amino acid sequence of the subunit of mitochondrial human liver aldehyde dehydrogenase is reported. It is the first structure determined for this enzyme type from any species, and isExpand
Human liver alcohol dehydrogenase
Determination of the amino acid sequence of the β1 subunit from the class I (pyrazole-sensitive) human liver alcohol dehydrogenase isoenzyme β1β1 revealed a 373-residue structure differing at 48Expand
Origin of the human alcohol dehydrogenase system: implications from the structure and properties of the octopus protein.
In contrast to the multiplicity of alcohol dehydrogenase in vertebrates, a class III type of the enzyme [i.e., a glutathione-dependent formaldehyde dehydrogenase; formaldehyde; NAD+ oxidoreductaseExpand
Cephalopod alcohol dehydrogenase: purification and enzymatic characterization
Octopus, squid and cuttle‐fish organs were examined for alcohol dehydrogenase activity. Only one form was detectable, with properties typical of mammalian class III alcohol dehydrogenase. TheExpand
Isolation, characterization and structure of subtilisin from a thermostable Bacillus subtilis isolate
A serine protease has been isolated and characterized from Bacillus subtilis, strain RT‐5 (a thermostable soil isolate from the Tharparkar desert of Pakistan) able to grow at 55°C. The primaryExpand
Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes.
The primary structure of class III alcohol dehydrogenase (dimeric with chi subunits) from human liver has been determined by peptide analyses. The protein chain is a clearly distinct type of subunitExpand
Comparison of three classes of human liver alcohol dehydrogenase. Emphasis on different substrate binding pockets.
Conformational models of the three characterized classes of mammalian liver alcohol dehydrogenase were constructed using computer graphics based on the known three-dimensional structure of the EExpand
Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain.
The primary structure of the gamma 1 subunit of human liver alcohol dehydrogenase isoenzyme gamma 1 gamma 1 was deduced by characterization of 36 tryptic and 2 CNBr peptides. The polypeptide chain isExpand
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