Výsledky vyhledávání - "W. F. Benisek"

High-efficiency incorporation in vivo of tyrosine analogues with altered hydroxyl acidity in place of the catalytic tyrosine-14 of Delta 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: effects of the modifications on isomerase kinetics

Autor: B, Brooks, R S, Phillips, W F, Benisek

Publikováno v: Biochemistry. 37(27)

Versions of the Y55F/Y88F modified form of Delta 5-3-ketosteroid isomerase in which the active-site tyrosine-14 is replaced by 2-fluorotyrosine, 3-fluorotyrosine, and 2,3-difluorotyrosine, amino acids having progressively greater acidity of their phe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::940d232abae4ac8269bd3c7b42a57e12
https://pubmed.ncbi.nlm.nih.gov/9657686

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Cloning, nucleotide sequence, and overexpression of the gene coding for delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B

Autor: Chae Youn Kim, Kwan Yong Choi, W. F. Benisek, Suhng Wook Kim

The structural gene coding for the delta 5-3-ketosteroid isomerase (KSI) of Pseudomonas putida biotype B has been cloned, and its entire nucleotide sequence has been determined by a dideoxynucleotide chain termination method. A 2.1-kb DNA fragment co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed043d445e7adbc9ecf5c2740804c27b
https://europepmc.org/articles/PMC197024/

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Extent of proton transfer in the transition states of the reaction catalyzed by the delta 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: site-specific replacement of the active site base, aspartate 38, by the weaker base alanine-3-sulfinate

Autor: C M, Holman, W F, Benisek

Publikováno v: Biochemistry. 33(9)

Previous studies of the mechanism of the steroid isomerase of Comamonas (Pseudomonas) testosteroni have identified aspartate 38 as the proton porter which transfers the substrate's 4 beta proton to the 6 beta position of the product. Consequently, as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::affc197b7a10504006f55eff0eeb9c2a
https://pubmed.ncbi.nlm.nih.gov/8117731

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Effect of protein concentration on the molecular weight of delta5-3-ketosteroid isomerase

Autor: E D Beckman, W F Tivol, W F Benisek

Publikováno v: Journal of Biological Chemistry. 250:271-275

The molecular weight of delta-5-3-ketosteroid isomerase from Pseudomonas testosteroni was determined by means of sedimentation equilibrium and exclusion chromatography over a wide range of enzyme concentrations in 0.2 M potassium phosphate buffer, pH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::476244bf944300d8fbdb935f1af06f9e
https://doi.org/10.1016/s0021-9258(19)42010-3

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Inactivation of phosphorylase b by potassium ferrate, a new reactive analogue of the phosphate group

Autor: Y M Lee, W F Benisek

Publikováno v: Journal of Biological Chemistry. 251:1553-1560

Rabbit muscle phosphorylase b reacts with the phosphate-like reagent potassium ferrate, K2FeO4, a potent oxidizing agent. The reaction results in inactivation of the enzyme and abolition of the ability of the enzyme to bind 5'-AMP. Activating and non

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::83dffa13cd2775611fadc207cd48cd0f
https://doi.org/10.1016/s0021-9258(17)33684-0

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The purification and characterization of delta 5-3-ketosteroid isomerase from Pseudomonas putida, a cysteine-containing isomerase

Autor: W F Benisek, J W Richards, S B Smith

Publikováno v: Journal of Biological Chemistry. 255:2678-2684

A delta 5-3-ketosteroid isomerase (EC 5.3.3.1) has been isolated from Pseudomonas putida Biotype B and purified to homogeneity. This previously undescribed steroid isomerase resembles that isolated from Pseudomonas testosteroni (Talalay, P., and Wang

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ecde19c40873ac7ba717605a03a7a60
https://doi.org/10.1016/s0021-9258(19)85789-7

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A novel chemical modification of delta 5-3-ketosteroid isomerase occurring during its 3-oxo-4-estren-17 beta-yl acetate-dependent photoinactivation

Autor: J R, Ogez, W F, Tivol, W F, Benisek

Publikováno v: The Journal of biological chemistry. 252(17)

The chemical change responsible for the 3-oxo-4-estren-17 beta-yl acetate-dependent photoinactivation of delta 5-3-ketosteroid isomerase has been identified by amino acid analysis and amino acid sequencing. Amino acid analysis of the enzyme and its p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::89eb071d92fe07e0c0ebfc80dc8d9b04
https://pubmed.ncbi.nlm.nih.gov/893400

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Inactivation of phosphorylase b by potassium ferrate. Identification of a tyrosine residue involved in the binding of adenosine 5'-monophosphate

Autor: Y M, Lee, W F, Benisek

Publikováno v: The Journal of biological chemistry. 253(15)

The site of reaction of potassium ferrate (K2FeO4) with rabbit muscle phosphorylase b has been further characterized in an extension of previously published studies (Lee, Y. M., and Benisek, W. F. (1976) J. Biol, Chem. 251, 1553-1560) reporting inact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5dc775860e43df5f1d1b41cad1406e5
https://pubmed.ncbi.nlm.nih.gov/670209

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Effect of protein concentration on the molecular weight of delta5-3-ketosteroid isomerase

Autor: W F, Tivol, E D, Beckman, W F, Benisek

Publikováno v: The Journal of biological chemistry. 250(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9a9c04787eca1ad7177ba33a8300085c
https://pubmed.ncbi.nlm.nih.gov/237889

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