M
M C Lorence
Researcher at University of Texas Southwestern Medical Center
Publications - 21
Citations - 1271
M C Lorence is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Complementary DNA & Gene. The author has an hindex of 16, co-authored 21 publications receiving 1239 citations. Previous affiliations of M C Lorence include University of Texas at Dallas & University of North Carolina at Chapel Hill.
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Journal ArticleDOI
Human 3β-Hydroxysteroid Dehydrogenase/ δ5→4Isomerase from Placenta: Expression in Nonsteroidogenic Cells of a Protein that Catalyzes the Dehydrogenation/Isomerization of C21 and C19 Steroids*
TL;DR: The isolation, cloning, and expression of a cDNA insert complementary to mRNA encoding human 3 beta-hydroxysteroid dehydrogenase/delta 5----4isomerase is reported, showing that the dehydrogenation/isomerization steps of steroid biosynthesis can be catalyzed by a single polypeptide chain, which can metabolize all of the major physiological substrates.
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Rat P45017α from Testis: Characterization of a Full-Length cDNA Encoding a Unique Steroid Hydroxylase Capable of Catalyzing Both Δ4- and Δ5-Steroid-17,20-Lyase Reactions
Fevold Hr,M C Lorence,McCarthy Jl,John M. Trant,Masaaki Kagimoto,Michael R. Waterman,J I Mason +6 more
TL;DR: A cDNA clone encoding the complete rat 17α-hydroxylase (P45017α) from testis has been identified and sequenced and the deduced amino acid sequence is found to have 69% similarity with human P45017 α, 64% similarities with bovine P 45017α, and 47% similarityWith chicken P452017α.
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Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins.
TL;DR: Site-directed mutagenesis was used to change the rare start codon, GTG, of putidaredoxin reductase to ATG which resulted in an 18-fold increase in the level of expression of this protein to 7.4 mg/g wet weight of cells.
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Expression of Messenger Ribonucleic Acid Species Encoding Steroidogenic Enzymes in Human Follicles and Corpora Lutea throughout the Menstrual Cycle
TL;DR: Levels of P450(17 alpha) mRNA in the human CL are consistent with the ability of the human, but not the bovine, CL to synthesize 17 alpha-hydroxyprogesterone and estrogens, and may suggest that CL estrogen biosynthesis is limited by 17alpha-hydroxylase or 17,20-lyase activities.
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Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis.
TL;DR: The results support the role of a carboxylic acid residue at position 302 in the catalytic activity of cytochrome P-450AROM, believed to be important in forming the substrate-binding pocket.