Kinetics of the isomerization of 5-androsten-3,17-dione catalyzed by delta 5-3-ketosteroid isomerase from Pseudomonas putida.
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This article is published in Journal of Biological Chemistry.The article was published on 1980-04-10 and is currently open access. It has received 11 citations till now. The article focuses on the topics: Pseudomonas putida & Isomerase.read more
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Mouse embryos contain polypeptide growth factor(s) capable of inducing a reversible neoplastic phenotype in nontransformed cells in culture.
TL;DR: The similarities of this mouse embryo‐derived growth factor to previously identified transforming growth factors suggest that both fetal development and neoplastic transformation may be affected by similar mechanisms.
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pH dependence of the kinetic parameters for 3-oxo-delta 5-steroid isomerase. Substrate catalysis and inhibition by (3S)-spiro[5 alpha-androstane-3,2'-oxiran]-17-one.
TL;DR: The similarity of the pH-rate profiles for isomerization of 4 and inhibition by 7 beta suggests that both reactions may be governed by the ionization state of the same carboxyl group of the enzyme.
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The 6-A crystal structure of delta 5-3-ketosteroid isomerase. Architecture and location of the active center.
TL;DR: The crystal structure of the dimeric steroid metabolizing enzyme, delta 5-3-ketosteroid isomerase (EC 5.3.1), has been solved to 6-A resolution by multiple isomorphous replacement, augmented by real space direct methods.
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A tale of two isomerases: compact versus extended active sites in ketosteroid isomerase and phosphoglucose isomerase.
Srinivas Somarowthu,Heather R. Brodkin,J. Alejandro D’Aquino,Dagmar Ringe,Mary Jo Ondrechen,Penny J. Beuning +5 more
TL;DR: Computational active site predictors, THEMATICS and POOL, were employed to identify functionally important residues that are not in direct contact with the reacting substrate molecule and demonstrate that, as predicted, remote residues are very important in PGI catalysis but make only small contributions to catalysis in KSI.
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Identification of active site residues by site-directed mutagenesis of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
Suhng Wook Kim,Kwan Yong Choi +1 more
TL;DR: Results indicate that active-site residues of the two homologous enzymes are similar, opposite to the previous identification of a cysteine in an active site-directed photoinactivation study of the delta 5-3-ketosteroid isomerase.
References
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The Determination of Enzyme Dissociation Constants
Hans Lineweaver,Dean Burk +1 more
TL;DR: On the basis of the assumed theory the rate of the observed reaction is directly proportional to the concentration of the enzyme-substrate compound, where (E:l = (ES).
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