Edith Wilson Miles

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Edith Wilson Miles
Born
Edith Margaret Wilson
Alma materUniversity of California, Berkeley
Scientific career
Thesis The bacterial metabolism of [alpha-methylserine and hydroxymethylserine] (1962)

Edith Wilson Miles (born Edith Margaret Wilson) is a biochemist known for her work on the structure and function of enzymes, especially her work on tryptophan synthase.

Contents

Education and career

Miles received her B.A. from the University of Texas at Austin in 1957, and then moved to the University of California, Berkeley where she earned a Ph.D. in 1962 [1] working in Esmond Emerson Snell's lab with Jesse Rabinowitz and Edward Adelberg as her advisors. [2] [3] With funding from the American Cancer Society, she moved to the University of Leicester as a postdoctoral researcher with Hans Kornberg. From 1964 until 1966, she was a postdoctoral investigator at Tufts University working with Alton Meister, and then she accepted an independent position at the National Institutes of Health. In 2000 she became a Scientist Emeritus. [1]

Research

Wilson's graduate research characterized an enzyme that required pyridoxal phosphate and tetrahydrofolate to convert α-methylserine to alanine and formaldehyde. [4] [5] Her subsequent work examined the glyoxylate cycle in bacterial cells and led to further investigation of enzymes that require pyridoxal phosphate. [6] Upon her move to the National Institutes of Health, she began to focus on tryptophan synthase, [7] [8] [9] first by establishing the mechanism of the enzyme [10] which would later allow her to investigate interactions between the subunits of the enzyme. [1] Wilson went on to use x-ray crystallography to obtain the structure of the enzyme, [11] [12] and used mutant forms of Salmonella typhimurium to identify the significant components of the enzyme. [1] She also showed that α2β2 complex of tryptophan synthase could unfold in the presence of guanine hydrochloride, [13] details about protein folding and shape that became relevant in later research about barrel-shaped proteins. [14] [15]

Selected publications

Awards and honors

While at the University of Texas at Austin, Miles (then known as Edith Margaret Wilson) was inducted into Alpha Lambda Delta, [16] [17] an honor society that recognizes achievement of first year university students and for which she later served as secretary. [18] In her senior year, 1957, she was elected to Phi Beta Kappa [19] : 170 and was a member of Mortar Board. [19] : 189  In 1994, Miles received the Hillebrand Award, named for William Francis Hillebrand, from the Chemical Society of Washington, a section of the American Chemical Society. [20]

Personal life

Her husband, H. Todd Miles, also worked at the National Institutes of Health and became Scientist Emeritus in 2000. [1]

Related Research Articles

<span class="mw-page-title-main">Tryptophan synthase</span> Class of enzymes

Tryptophan synthase or tryptophan synthetase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. However, it is absent from Animalia. It is typically found as an α2β2 tetramer. The α subunits catalyze the reversible formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Each α active site is connected to a β active site by a 25 Ångstrom long hydrophobic channel contained within the enzyme. This facilitates the diffusion of indole formed at α active sites directly to β active sites in a process known as substrate channeling. The active sites of tryptophan synthase are allosterically coupled.

<span class="mw-page-title-main">Glycogen phosphorylase</span> Class of enzymes

Glycogen phosphorylase is one of the phosphorylase enzymes. Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.

<span class="mw-page-title-main">Phosphoribosyl pyrophosphate</span> Chemical compound

Phosphoribosyl pyrophosphate (PRPP) is a pentose phosphate. It is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, as well as in pyrimidine nucleotide formation. Hence it is a building block for DNA and RNA. The vitamins thiamine and cobalamin, and the amino acid tryptophan also contain fragments derived from PRPP. It is formed from ribose 5-phosphate (R5P) by the enzyme ribose-phosphate diphosphokinase:

Alkylglycerone phosphate synthase is an enzyme associated with Type 3 Rhizomelic chondrodysplasia punctata. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Serine hydroxymethyltransferase</span> InterPro Family

Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-methylenetetrahydrofolate (5,10-CH2-THF). This reaction provides the largest part of the one-carbon units available to the cell.

Amine <i>N</i>-methyltransferase Class of enzymes

Amine N-methyltransferase, also called indolethylamine N-methyltransferase, and thioether S-methyltransferase, is an enzyme that is ubiquitously present in non-neural tissues and catalyzes the N-methylation of tryptamine and structurally related compounds. More recently, it was discovered that this enzyme can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.

<span class="mw-page-title-main">Phosphoribosylanthranilate isomerase</span> Enzyme involved in tryptophan synthesis

In enzymology, a phosphoribosylanthranilate isomerase (PRAI) is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan.

<span class="mw-page-title-main">Anthranilate synthase</span>

The enzyme anthranilate synthase catalyzes the chemical reaction

<span class="mw-page-title-main">Tryptophanase</span> Enzyme that converts tryptophan into indole

The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

<span class="mw-page-title-main">Chorismate synthase</span>

The enzyme chorismate synthase catalyzes the chemical reaction

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cystathionine gamma-synthase</span> Class of enzymes

In enzymology, a cystathionine gamma-synthase is an enzyme that catalyzes the formation of cystathionine from cysteine and an activated derivative of homoserine, e.g.:

<span class="mw-page-title-main">Nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase</span> Class of enzymes

In enzymology, a nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Mary Jane Osborn</span> American biochemist and molecular biologist (1927–2019)

Mary Jane Osborn was an American biochemist and microbiologist known for her research on the biosynthesis of lipopolysaccharide, a key component of the outer membrane of Gram-negative bacteria, and discovering the mechanism of action of the anti-cancer drug methotrexate. She headed the Department of Molecular Biology and Biophysics at the University of Connecticut Health Center and served as president of the American Society for Biochemistry and Molecular Biology.

<span class="mw-page-title-main">Sulfometuron methyl</span> Chemical compound

Sulfometuron methyl is an organic compound used as a herbicide. It is classed as a sulfonylurea. It functions via the inhibitition of acetolactate synthase enzyme, which catalyses the first step in biosynthesis of the branched-chain amino acids valine, leucine and isoleucine.

Esmond Emerson Snell (September 22, 1914 – December 9, 2003) was an American biochemist who spent his career researching vitamins and nutritional requirements of bacteria and yeast. He is well known for his study of lactic acid-producing bacteria, developing microbiological assays for a number of key nutrients; the discovery of more than half of known vitamins has been attributed to the use of this work. He discovered several B vitamins, including folic acid, and characterized the biochemistry of vitamin B6 (also known as pyrixodal).

Charles Clifton Richardson is an American biochemist and professor at Harvard University. Richardson received his undergraduate education at Duke University, where he majored in medicine. He received his M.D. at Duke Medical School in 1960. Richardson works as a professor at Harvard Medical School, and he served as editor/associate editor of the Annual Review of Biochemistry from 1972 to 2003. Richardson received the American Chemical Society Award in Biological Chemistry in 1968, as well as numerous other accolades.

<span class="mw-page-title-main">George Stark</span>

George Stark is an American chemist and biochemist. His research interests include protein and enzyme function and modification, interferons and cytokines, signal transduction, and gene expression.

Beverly Marie Guirard was a microbiologist who worked on the biochemistry of microbial growth, especially with respect to vitamin B6. She is also known for her work defining the components of coenzyme A which was a part of the research that led to a Nobel Prize for Fritz Albert Lipmann.

<span class="mw-page-title-main">Bettie Sue Masters</span> American biochemist

Bettie Sue Siler Masters is an adjunct professor at Duke University known for her work on nitric oxide synthase and cytochrome P450 reductase. She was the 1992 recipient of the FASEB Excellence in Science Award, and has been elected as a member of the National Academy of Medicine and as a fellow of the American Association for the Advancement of Science.

References

  1. 1 2 3 4 5 Miles, Edith Wilson (April 5, 2013). "The Tryptophan Synthase α2β2 Complex: A Model for Substrate Channeling, Allosteric Communication, and Pyridoxal Phosphate Catalysis". Journal of Biological Chemistry. 288 (14): 10084–10091. doi: 10.1074/jbc.X113.463331 . ISSN   0021-9258. PMC   3617248 . PMID   23426371.
  2. ↑ Snell, Esmond E. (1993). "FROM BACTERIAL NUTRITION TO ENZYME STRUCTURE: A Personal Odyssey". Annual Review of Biochemistry. 62 (1): 1–26. doi: 10.1146/annurev.bi.62.070193.000245 . ISSN   0066-4154. PMID   8352584.
  3. ↑ Miles, Edith Wilson; Metzler, David E. (November 1, 2004). "Esmond Emerson Snell (1914–2003)". The Journal of Nutrition. 134 (11): 2907–2910. doi: 10.1093/jn/134.11.2907 . ISSN   0022-3166. PMID   15514250.
  4. ↑ Wilson, Edith M.; Snell, Esmond E. (1962). "Metabolism of α-Methylserine". Journal of Biological Chemistry. 237 (10): 3171–3179. doi: 10.1016/s0021-9258(18)50139-3 . ISSN   0021-9258.
  5. ↑ Wilson, Edith M.; Snell, Esmond E. (1962). "Metabolism of α-Methylserine". Journal of Biological Chemistry. 237 (10): 3180–3184. doi: 10.1016/s0021-9258(18)50140-x . ISSN   0021-9258.
  6. ↑ WILSON, EM; KORNBERG, HL (September 1, 1963). "PROPERTIES OF CRYSTALLINE l-ASPARTATE 4-CARBOXY-LYASE FROM ACHROMOBACTER SP". Biochemical Journal. 88 (3): 578–587. doi:10.1042/bj0880578. ISSN   0006-2936. PMC   1202217 . PMID   14071532.
  7. ↑ Miles, Edith Wilson (1991). "Structural basis for catalysis by tryptophan synthase". Advances in enzymology : and related areas of molecular biology. Vol.64. Vol. 64. NewYork ; Chichester: Wiley. pp. 93–172. ISBN   978-0-471-50949-3.
  8. ↑ Miles, Edith Wilson (1991). "Tryptophan synthase: structure, function, and subunit interaction". Advances in enzymology : and related areas of molecular biology. Vol.64. Vol. 49. NewYork ; Chichester: Wiley. pp. 127–. ISBN   978-0-471-50949-3.
  9. ↑ "Chapter 8 Tryptophan synthase structure, function, and protein engineering". Subcellular biochemistry. Vol.24, Proteins: structure, function and engineering. New York ; London: Plenum. 1995. pp. 207–254. ISBN   978-0-306-44846-1.
  10. ↑ Miles, Edith Wilson.; Hatanaka, M.; Crawford, I. P. (August 1, 1968). "A new thiol-dependent transamination reaction catalyzed by the B protein of Escherichia coli tryptophan synthetase". Biochemistry. 7 (8): 2742–2753. doi:10.1021/bi00848a008. ISSN   0006-2960. PMID   4877071.
  11. ↑ Ahmed, S A; Miles, E W; Davies, D R (1985). "Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium". Journal of Biological Chemistry. 260 (6): 3716–3718. doi: 10.1016/s0021-9258(19)83682-7 . ISSN   0021-9258. PMID   3882715.
  12. ↑ Hyde, C C; Ahmed, S A; Padlan, E A; Miles, E W; Davies, D R (1988). "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium". Journal of Biological Chemistry. 263 (33): 17857–17871. doi: 10.1016/s0021-9258(19)77913-7 . ISSN   0021-9258. PMID   3053720.
  13. ↑ Miles, Edith Wilson; Yutani, Katsuhide; Ogasahara, Kyoko (May 25, 1982). "Guanidine hydrochloride-induced unfolding of the .alpha. subunit of tryptophan synthase and of the two .alpha. proteolytic fragments: evidence for stepwise unfolding of the two .alpha. domains". Biochemistry. 21 (11): 2586–2592. doi:10.1021/bi00540a002. ISSN   0006-2960. PMID   7046790.
  14. ↑ Miles, Edith Wilson; Davies, David R. (2000). "On the Ancestry of Barrels". Science. 289 (5484): 1490. doi:10.1126/science.289.5484.1490. ISSN   0036-8075. JSTOR   3077778. PMID   10991737. S2CID   82637907.
  15. ↑ "Protein Clipping in Lab and Cell". Science News. 113 (17): 279–280. 1978. doi:10.2307/3962872. ISSN   0036-8423. JSTOR   3962872.
  16. ↑ "Alpha Lambda Delta - Honorary scholastic fraternity for freshman". University of Texas at Austin. Archived from the original on January 9, 2022. Retrieved January 9, 2022.
  17. ↑ University Of Texas At Austin (1955). Cactus Yearbook, 1955. University of Texas at Austin. p. 283. doi:10.15781/T2ZG6GP6H.
  18. ↑ University Of Texas At Austin (1956). Cactus Yearbook, 1956. University of Texas at Austin. p. 167. doi:10.15781/T23776B01.
  19. 1 2 University Of Texas At Austin (1957). Cactus Yearbook, 1957. University of Texas at Austin. p. 167. doi:10.15781/T23776B01. hdl:2152/61517.
  20. ↑ "Past Awardees of the CSW Hillebrand Award" (PDF). The Capital Chemist. Vol. 59, no. 6. 2009 [August/September 2009]. Retrieved January 9, 2022.
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