Patrick J. Stover

Last updated
Patrick J. Stover
Born1964 (age 59–60)
CitizenshipUS
Education
PartnerDenise Stover
Children4
Scientific career
Institutions

Patrick J. Stover (born 1964) is an American nutrition scientist who researches B vitamins. He is a fellow of the American Association for the Advancement of Science and a member of the National Academy of Sciences. He has been co-editor of the Annual Review of Nutrition since 2015.

Contents

Early life and education

Patrick J. Stover was born in 1964 to parents Katherine Hanlon and William Stover. His father, William H. Stover, was a decorated WWII veteran. As a Private First Class in the 1st Marine Division, he was awarded the Silver Star from the president of the United States “for conspicuous gallantry and intrepidity during action against enemy Japanese forces on Guadalcanal, Solomon Islands on November 3, 1942". [1]

Stover grew up in rural Pennsylvania and he and his siblings were first generation college students. [2] [3] He attended Saint Joseph's University in Pennsylvania, graduating with a bachelor's degree in chemistry in 1986. He then graduated from VCU Medical Center in 1990 with a PhD in biochemistry and molecular biophysics. [4] [5]

Career

Much of Stover's research centers on the B vitamins folate, vitamin B12 and riboflavin. [4] Following the completion of his PhD, Stover had two postdoctoral appointments. The first was at VCU Medical Center from 1990 to 1991 with his PhD advisor Verne Schirch. Next, he went to the University of California, Berkeley to work with Barry Shane from 1992 to 1994. He was hired at Cornell University as an assistant professor in the nutritional sciences division in 1994 and was appointed to associate professor in 2000. In 2005, he was promoted once more to professor. [6] In 2018, he was hired to serve as the Vice Chancellor and Dean for the College of Agriculture and Life Sciences at Texas A&M University and director of Texas A&M AgriLife Research. [7] He has been co-editor of the Annual Review of Nutrition since 2015. [8]

He has made several fundamental discoveries by identifying new pathways in the field of folate biochemistry. These discoveries include identification of the pathway for the synthesis of 5-formyltetrahydrfolate, otherwise known as lucovorin, [9] the regulation of folate metabolism by iron, [10] [11] [12] the presence of de novo thymidylate biosynthesis in mitochondria including discovery of a novel isozyme of dihydrofolate reductase, [13] and the role of sumoylation in nuclear folate metabolism. [14] [15]  His research group also identified impaired de novo thymidylate biosynthesis in the etiology of folic acid-responsive neural tube defects including spina bifida in mouse models. [16]  He has participated on many panels and expert committees related to folic acid fortification of the food supply and neural tube defect prevention. [17]

Awards and honors

He received a Presidential Early Career Award for Scientists and Engineers from President Bill Clinton in 1996. The American Association for the Advancement of Science elected him as a fellow in 2014. [4] He served as president of the American Society for Nutrition from 2015 to 2016. [6] In 2016 he was elected as a member of the National Academy of Sciences. [4]

Personal life

He is married to Denise Stover; the Stovers have four children, all of whom attended Cornell University. [7]

Related Research Articles

<span class="mw-page-title-main">Folate</span> Vitamin B9; nutrient essential for DNA synthesis

Folate, also known as vitamin B9 and folacin, is one of the B vitamins. Manufactured folic acid, which is converted into folate by the body, is used as a dietary supplement and in food fortification as it is more stable during processing and storage. Folate is required for the body to make DNA and RNA and metabolise amino acids necessary for cell division and maturation of blood cells. As the human body cannot make folate, it is required in the diet, making it an essential nutrient. It occurs naturally in many foods. The recommended adult daily intake of folate in the U.S. is 400 micrograms from foods or dietary supplements.

<span class="mw-page-title-main">Sphingolipid</span> Family of chemical compounds

Sphingolipids are a class of lipids containing a backbone of sphingoid bases, which are a set of aliphatic amino alcohols that includes sphingosine. They were discovered in brain extracts in the 1870s and were named after the mythological sphinx because of their enigmatic nature. These compounds play important roles in signal transduction and cell recognition. Sphingolipidoses, or disorders of sphingolipid metabolism, have particular impact on neural tissue. A sphingolipid with a terminal hydroxyl group is a ceramide. Other common groups bonded to the terminal oxygen atom include phosphocholine, yielding a sphingomyelin, and various sugar monomers or dimers, yielding cerebrosides and globosides, respectively. Cerebrosides and globosides are collectively known as glycosphingolipids.

In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

In biochemistry, lipogenesis is the conversion of fatty acids and glycerol into fats, or a metabolic process through which acetyl-CoA is converted to triglyceride for storage in fat. Lipogenesis encompasses both fatty acid and triglyceride synthesis, with the latter being the process by which fatty acids are esterified to glycerol before being packaged into very-low-density lipoprotein (VLDL). Fatty acids are produced in the cytoplasm of cells by repeatedly adding two-carbon units to acetyl-CoA. Triacylglycerol synthesis, on the other hand, occurs in the endoplasmic reticulum membrane of cells by bonding three fatty acid molecules to a glycerol molecule. Both processes take place mainly in liver and adipose tissue. Nevertheless, it also occurs to some extent in other tissues such as the gut and kidney. A review on lipogenesis in the brain was published in 2008 by Lopez and Vidal-Puig. After being packaged into VLDL in the liver, the resulting lipoprotein is then secreted directly into the blood for delivery to peripheral tissues.

Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems.

<span class="mw-page-title-main">Coenzyme M</span> Chemical compound

Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaeal methanogens, and in the metabolism of other substrates in bacteria. It is also a necessary cofactor in the metabolic pathway of alkene-oxidizing bacteria. CoM helps eliminate the toxic epoxides formed from the oxidation of alkenes such as propylene. The structure of this coenzyme was discovered by CD Taylor and RS Wolfe in 1974 while they were studying methanogenesis, the process by which carbon dioxide is transformed into methane in some archaea. The coenzyme is an anion with the formula HSCH
2CH
2SO−
3. It is named 2-mercaptoethanesulfonate and abbreviated HS–CoM. The cation is unimportant, but the sodium salt is most available. Mercaptoethanesulfonate contains both a thiol, which is the main site of reactivity, and a sulfonate group, which confers solubility in aqueous media.

<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.

<span class="mw-page-title-main">5,10-Methylenetetrahydrofolate</span> Chemical compound

5,10-Methylenetetrahydrofolate (N5,N10-Methylenetetrahydrofolate; 5,10-CH2-THF) is cofactor in several biochemical reactions. It exists in nature as the diastereoisomer [6R]-5,10-methylene-THF.

<span class="mw-page-title-main">Phosphatidylethanolamine N-methyltransferase</span> Protein-coding gene in the species Homo sapiens

Phosphatidylethanolamine N-methyltransferase is a transferase enzyme which converts phosphatidylethanolamine (PE) to phosphatidylcholine (PC) in the liver. In humans it is encoded by the PEMT gene within the Smith–Magenis syndrome region on chromosome 17.

<span class="mw-page-title-main">Sterol regulatory element-binding protein 1</span> Protein-coding gene in the species Homo sapiens

Sterol regulatory element-binding transcription factor 1 (SREBF1) also known as sterol regulatory element-binding protein 1 (SREBP-1) is a protein that in humans is encoded by the SREBF1 gene.

<span class="mw-page-title-main">Serine C-palmitoyltransferase</span>

In enzymology, a serine C-palmitoyltransferase (EC 2.3.1.50) is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">MAP3K2</span> Protein-coding gene in the species Homo sapiens

Mitogen-Activated Protein Kinase Kinase Kinase 2 also known as MEKK2 is an enzyme that in humans is encoded by the MAP3K2 gene.

<span class="mw-page-title-main">Phosphoglycerate dehydrogenase</span> Metabolic enzyme PHGDH

Phosphoglycerate dehydrogenase (PHGDH) is an enzyme that catalyzes the chemical reactions

Phosphatidylinositol 5-phosphate (PtdIns5P) is a phosphoinositide, one of the phosphorylated derivatives of phosphatidylinositol (PtdIns), that are well-established membrane-anchored regulatory molecules. Phosphoinositides participate in signaling events that control cytoskeletal dynamics, intracellular membrane trafficking, cell proliferation and many other cellular functions. Generally, phosphoinositides transduce signals by recruiting specific phosphoinositide-binding proteins to intracellular membranes.

<span class="mw-page-title-main">Stephen J. Benkovic</span> American chemist

Stephen James Benkovic is an American chemist known for his contributions to the field of enzymology. He holds the Evan Pugh University Professorship and Eberly Chair in Chemistry at The Pennsylvania State University. He has developed boron compounds that are active pharmacophores against a variety of diseases. Benkovic has concentrated on the assembly and kinetic attributes of the enzymatic machinery that performs DNA replication, DNA repair, and purine biosynthesis.

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

The purinosome is a putative multi-enzyme complex that carries out de novo purine biosynthesis within the cell. It is postulated to include all six of the human enzymes identified as direct participants in this ten-step biosynthetic pathway converting phosphoribosyl pyrophosphate to inosine monophosphate:

Rowena Green Matthews, born in 1938, is the G. Robert Greenberg Distinguished University professor emeritus at the University of Michigan, Ann Arbor. Her research focuses on the role of organic cofactors as partners of enzymes catalyzing difficult biochemical reactions, especially folic acid and cobalamin. Among other honors, she was elected to the National Academy of Sciences in 2002 and the Institute of Medicine in 2004.

The Reduced Folate Carrier (RFC) Family is a group of transport proteins that is part of the major facilitator superfamily. RFCs take up folate, reduced folate, derivatives of reduced folate and the drug, methotrexate.

The folate-biopterin transporter (FBT) family (TC# 2.A.71) is a distant family within the major facilitator superfamily, most closely related to drug resistance permeases. Proteins of the FBT family are reported to contain about 480 to 650 amino acyl residues. All probably have 12 transmembrane α-helical segments (TMSs). They may function by H+ symport.

Morphinone reductase is an enzyme which catalyzes the NADH-dependent saturation of the carbon-carbon double bond of morphinone and codeinone, yielding hydromorphone and hydrocodone respectively. This saturation reaction is assisted by a FMN cofactor and the enzyme is a member of the α/β-barrel flavoprotein family. The sequence of the enzyme has been obtained from bacteria Pseudomonas putida M10 and has been successfully expressed in yeast and other bacterial species. The enzyme is reported to harbor high sequence and structural similarity to the Old Yellow Enzyme, a large group of flavin-dependent redox biocatalysts of yeast species, and an oestrogen-binding protein of Candida albicans. The enzyme has demonstrated value in biosynthesis of semi-opiate drugs in microorganisms, expanding the chemical diversity of BIA biosynthesis.

References

  1. ↑ "William Stover - Recipient -". valor.militarytimes.com. Retrieved 2021-01-22.
  2. ↑ "William H. J. Stover". The Philadelphia Inquirer. 7 July 2001. p. 10. Retrieved 11 January 2021.
  3. ↑ "Patrick J. Stover, PhD". Texas A&M College of Agriculture & Life Sciences. Retrieved 11 January 2021.
  4. 1 2 3 4 "Patrick Stover". National Academy of Sciences. Retrieved 11 January 2021.
  5. ↑ "Patrick Stover". Cornell University. 2015. Retrieved 11 January 2021.
  6. 1 2 "Patrick J. Stover, PhD" (PDF). Texas A&M Agrilife. 2017. Retrieved 11 January 2021.
  7. 1 2 "TEXAS A&M HIRES NEW LEADER OF AGRICULTURE COLLEGE, AGENCIES". Texas A&M University. 8 February 2018. Retrieved 11 January 2021.
  8. ↑ Stover, Patrick J.; Bowman, Barbara (2015). "Introduction". Annual Review of Nutrition. 35. doi:10.1146/annurev-nu-35-071715-100001.
  9. ↑ Stover, P.; Schirch, V. (1990-08-25). "Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate". The Journal of Biological Chemistry. 265 (24): 14227–14233. doi: 10.1016/S0021-9258(18)77290-6 . ISSN   0021-9258. PMID   2201683.
  10. ↑ Fox, Jennifer T.; Stover, Patrick J. (2009-11-06). "Mechanism of the internal ribosome entry site-mediated translation of serine hydroxymethyltransferase 1". The Journal of Biological Chemistry. 284 (45): 31085–31096. doi: 10.1074/jbc.M109.035576 . ISSN   1083-351X. PMC   2781508 . PMID   19734143.
  11. ↑ Woeller, Collynn F.; Fox, Jennifer T.; Perry, Cheryll; Stover, Patrick J. (2007-10-12). "A ferritin-responsive internal ribosome entry site regulates folate metabolism". The Journal of Biological Chemistry. 282 (41): 29927–29935. doi: 10.1074/jbc.M706264200 . ISSN   0021-9258. PMID   17702748.
  12. ↑ Oppenheim, E. W.; Adelman, C.; Liu, X.; Stover, P. J. (2001-06-08). "Heavy chain ferritin enhances serine hydroxymethyltransferase expression and de novo thymidine biosynthesis". The Journal of Biological Chemistry. 276 (23): 19855–19861. doi: 10.1074/jbc.M100039200 . ISSN   0021-9258. PMID   11278996.
  13. ↑ Anderson, Donald D.; Quintero, Cynthia M.; Stover, Patrick J. (2011-09-13). "Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria". Proceedings of the National Academy of Sciences of the United States of America. 108 (37): 15163–15168. Bibcode:2011PNAS..10815163A. doi: 10.1073/pnas.1103623108 . ISSN   1091-6490. PMC   3174652 . PMID   21876188.
  14. ↑ Anderson, Donald D.; Woeller, Collynn F.; Chiang, En-Pei; Shane, Barry; Stover, Patrick J. (2012-03-02). "Serine hydroxymethyltransferase anchors de novo thymidylate synthesis pathway to nuclear lamina for DNA synthesis". The Journal of Biological Chemistry. 287 (10): 7051–7062. doi: 10.1074/jbc.M111.333120 . ISSN   1083-351X. PMC   3293584 . PMID   22235121.
  15. ↑ MacFarlane, Amanda J.; Anderson, Donald D.; Flodby, Per; Perry, Cheryll A.; Allen, Robert H.; Stabler, Sally P.; Stover, Patrick J. (2011-12-23). "Nuclear localization of de novo thymidylate biosynthesis pathway is required to prevent uracil accumulation in DNA". The Journal of Biological Chemistry. 286 (51): 44015–44022. doi: 10.1074/jbc.M111.307629 . ISSN   1083-351X. PMC   3243516 . PMID   22057276.
  16. ↑ Beaudin, Anna E.; Abarinov, Elena V.; Noden, Drew M.; Perry, Cheryll A.; Chu, Stephanie; Stabler, Sally P.; Allen, Robert H.; Stover, Patrick J. (April 2011). "Shmt1 and de novo thymidylate biosynthesis underlie folate-responsive neural tube defects in mice". The American Journal of Clinical Nutrition. 93 (4): 789–798. doi:10.3945/ajcn.110.002766. ISSN   1938-3207. PMC   3057548 . PMID   21346092.
  17. ↑ Field, Martha S.; Stover, Patrick J. (February 2018). "Safety of folic acid". Annals of the New York Academy of Sciences. 1414 (1): 59–71. Bibcode:2018NYASA1414...59F. doi:10.1111/nyas.13499. ISSN   1749-6632. PMC   5849489 . PMID   29155442.
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