John Westley | |
---|---|
Born | 1927 |
Education | University of Chicago (Ph.D. 1954) |
Known for | Studies of enzyme kinetics, especially of sulfurtransferases |
Scientific career | |
Fields | Biochemistry |
Institutions | University of Chicago |
Thesis | Studies on the synthesis of histidine by Escherichia coli (1954) |
Notes | |
A photograph may be found at https://photoarchive.lib.uchicago.edu/db.xqy?one=apf1-13257.xml, but cannot be displayed here on account of copyright restrictions |
John W. Westley (1927–) [1] was an enzymologist at the University of Chicago, best known for his research on rhodanese and other sulfurtransferases.
John Westley obtained his Ph.D. in 1954 at the University of Chicago on the basis of a thesis entitled "Studies on the synthesis of histidine by Escherichia coli". [1] He subsequently worked in the Department of Biochemistry (now Department of Biochemistry & Molecular Biology) of the University of Chicago.
John Westley's doctoral research concerned the biosynthesis of histidine in Escherichia coli. Subsequently he became an enzymologist and worked principally on rhodanese (thiosulfate sulfurtransferase, EC 2.8.1.1), starting with a comparison of the enzyme forms isolated from beef liver and kidney [2] and purification of the kidney enzyme. [3]
He continued to study the kinetic behaviour of the liver enzyme, [4] and was probably the first to study memory effects in substituted-enzyme ("ping-pong") mechanisms. [5] [6] Memory effects are also possible in ternary-complex mechanisms, as in the "mnemonical model" used by Ricard and co-workers to explain the deviations from linear kinetics observed in wheat-germ hexokinase. [7] However, the kinetic effects are completely different. The memory effects discussed by Katz and Westley, [6] do not generate departures from linear kinetics but instead allow an enzyme to "remember" which of various alternative substrates it handled in the previous catalytic and modify its kinetic properties accordingly. In addition to specific reports on sulfurtransferases he wrotre a review on these enzymes. [8]
Westley was also concerned with more general aspects of enzyme kinetics, such as uncompetitive inhibition in metabolic systems, [9] metabolite channelling, [10] and rapid-equilibrium mechanisms, [11] and regulation. [12]
In addition to his research publications, Westley is also known for his book Enzymic catalysis, [13] which in its time was the leading textbook on the subject.
Irwin Allan Rose was an American biologist. Along with Aaron Ciechanover and Avram Hershko, he was awarded the 2004 Nobel Prize in Chemistry for the discovery of ubiquitin-mediated protein degradation.
Robert Arnold Alberty (1921–2014) was an American biophysical chemist, professor emeritus at the Massachusetts Institute of Technology, and a member of the National Academy of Sciences.
The branched-chain α-ketoacid dehydrogenase complex is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family, which also includes pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle.
In enzymology, aldose reductase is an enzyme in humans encoded by the gene AKR1B1. It is an cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides, and primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism.
William Wallace Cleland (January 6, 1930 – March 6, 2013, often cited as W. W. Cleland, and known almost universally as "Mo Cleland", was a University of Wisconsin-Madison biochemistry professor. His research was concerned with enzyme reaction mechanism and enzyme kinetics, especially multiple-substrate enzymes. He was elected to the National Academy of Sciences in 1985.
In enzymology, histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction
Hydroxyprostaglandin dehydrogenase 15-(NAD) (the HUGO-approved symbol = HPGD; HGNC ID, HGNC:5154), also called 15-hydroxyprostaglandin dehydrogenase (NAD+), (EC 1.1.1.141), is an enzyme that catalyzes the following chemical reaction:
In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a NADPH—hemoprotein reductase is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-mercaptopyruvate sulfurtransferase is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.
In enzymology, a thiosulfate-thiol sulfurtransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a tRNA sulfurtransferase is an enzyme that catalyzes the chemical reaction
The enzyme chorismate synthase catalyzes the chemical reaction
In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction
Thiosulfate sulfurtransferase is an enzyme that in humans is encoded by the TST gene.
Vincent Massey was an Australian biochemist and enzymologist best known for his contributions to the study of flavoenzymes. He was elected to the National Academy of Sciences in 1995 for his use of physical biochemistry to relate flavin chemistry to flavin enzymology.
Gösta Pettersson is an emeritus professor in biochemistry at Lund University, Sweden. He was born in 1937 in Varberg, Sweden. He gained his Ph.D. at Lund University in 1966 on the basis of a thesis on toluquinones, and his early research was mainly concerned with fumigatin and other products of fungal metabolism.
Daniel Edward Atkinson was an American biochemist who worked at UCLA for 40 years from 1952 until his retirement in 1992, though he continued his scientific work as Emeritus Professor. He is best known for the concept of energy charge.
Enzyme memory is a concept in enzyme kinetics based on the idea that the kinetic properties of an enzyme may vary according to conditions in its previous catalytic cycle. It can occur both in ternary-complex mechanisms and in substituted-enzyme ("ping-pong") mechanisms, with very different consequences.