Beverly Guirard

Last updated
Beverly Guirard
BornDecember 10, 1915 [1]
St. Martinville, Louisiana
DiedJanuary 17, 2006(2006-01-17) (aged 90)
Alma materUniversity of Texas
Scientific career
Thesis The nutritional role of acetate for lactic acid bacteria  (1945)
Doctoral advisor Roger J. Williams

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.

Contents

Education and career

Guirard grew up in Louisiana and went to high school in St. Martinville, Louisiana. [2] Guirard received a B.S. from Southwestern Louisiana Institute in 1936, and a masters degree from Louisiana State University in 1938. [3] She went on to earn a Ph.D. from the University of Texas in 1945 where she worked on lactic acid bacteria and their conversion of acetate into lipids and steroidal material, [4] research which built upon Esmond Emerson Snell's earliest work that identified acetate as a key factor leading to reliable growth of microorganisms. [5] After her Ph.D. she remained at the University of Texas, where she joined Snell's lab in 1951. [6] She moved with the lab to the University of California, Berkeley in 1956, and then returned to Texas in 1976 where she worked until her retirement in 1990. [6] [3]

Research

Guirard is known for her research into the biochemical compounds determining microbial growth, especially vitamins and amino acids. Her early research determined how to isolate vitamins from tissue extracts. [7] During her Ph.D, Guirard established how acetate stimulated growth of the bacteria Lactobacillus casei. [8] [9] She went on to use bacteria to determine the levels of amino acids inside cells, [10] and worked with Robert Wagner on synthesis of pantothenic acid in his model system of the fungus Neurospora . [11]

Guirard worked with Fritz Albert Lipmann who won the 1953 Nobel Prize for the discovery of coenzyme A. During the research that led to the discovery of coenzyme A, Lipmann used pig liver's as a source for the coenzyme. As Lipmann [12] [13] and others have described, [14] Guirard examined this material and discovered that the vitamin pantothenic acid only appeared after extended enzymatic activity. She confirmed this observation by hydrolyzing the coenzyme into adenylic acid and Β-alanine and thereby demonstrating that the vitamin pantothenic acid was a part of the coenzyme; this work was published with Lipmann, Nathan Kaplan, Constance Tuttle, and G. David Novelli in 1947. [15] A second publication provided more details on how to prepare coenyzme A with details on its vitamin content and structure. [16] Later, Kaplan detailed Guirard's experiments and noted her repeated investigations into the samples she received, and how it was only through her extended curiosity that she was able to identify the presence of pantothenic acid within conenzyme A. [17] Lipmann also describes Guirard's expertise in finding pantothenic acid in tissue extracts, and how this led to the observation that an enzyme removed pantothenic acid from coenzyme A. [18] In 1953, Lipmann reviewed the chemistry and function of coenyzme A and he noted it was 'through [Guirard]'s skillful observations that pantothenic acid was detected in the coenzyme". [19]

Guirard was a long-time associate of Esmond Emerson Snell, and was a part of the team that discovered the different forms of vitamin B6. [6] [20] [21] Her work in this realm included investigations into enzymes including ornithine decarboxylase [22] and histidine decarboxylase. [23] [24] [25] She established the amino acids, [26] vitamins, [27] or combination of amino acids and vitamins required for microbial growth. [28] [29] She also used microbial growth as an assay to determine the effectiveness of anti-tumor agents, [30] and examined the role of polyamines such as spermine and spermidine on cell growth. [31]

Selected publications

Personal life

The Beverly Guirard endowment at the University Catholic Center in Austin, Texas was established in honor of Guirard. [32] [33]

Related Research Articles

<span class="mw-page-title-main">Pantothenic acid</span> Chemical compound

Pantothenic acid (vitamin B5) is a B vitamin and an essential nutrient. All animals need pantothenic acid in order to synthesize coenzyme A (CoA)—essential for metabolizing fatty acid—and to synthesize and metabolize proteins, carbohydrates, and fats.

<span class="mw-page-title-main">Biotin</span> Chemical compound (vitamin B7)

Biotin (also known as vitamin B7 or vitamin H) is one of the B vitamins. It is involved in a wide range of metabolic processes, both in humans and in other organisms, primarily related to the utilization of fats, carbohydrates, and amino acids. The name biotin, borrowed from the German Biotin, derives from the Ancient Greek word βίοτος (bíotos; 'life') and the suffix "-in" (a suffix used in chemistry usually to indicate 'forming'). Biotin appears as a white crystalline solid that looks like needles.

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

Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO− form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential only for infants, it has now been shown in longer-term studies to be essential for adults also. It is encoded by the codons CAU and CAC.

<span class="mw-page-title-main">Coenzyme A</span> Coenzyme, notable for its synthesis and oxidation role

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP).

<span class="mw-page-title-main">Acetyl-CoA</span> Chemical compound

Acetyl-CoA is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. Its main function is to deliver the acetyl group to the citric acid cycle to be oxidized for energy production.

B vitamins are a class of water-soluble vitamins that play important roles in cell metabolism and synthesis of red blood cells. They are a chemically diverse class of compounds, but are associated in diet, often occurring together in the same foods. Dietary supplements containing all eight are referred to as a vitamin B complex. Individual B vitamins are referred to by B-number or by chemical name, such as B1 for thiamine, B2 for riboflavin, and B3 for niacin, while some are more commonly recognized by name than by number, such as pantothenic acid (B5), biotin (B7), and folate (B9).

<span class="mw-page-title-main">Cofactor (biochemistry)</span> Non-protein chemical compound or metallic ion

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.

β-Alanine Chemical compound

β-Alanine is a naturally occurring beta amino acid, which is an amino acid in which the amino group is attached to the β-carbon instead of the more usual α-carbon for alanine (α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid. Unlike its counterpart α-alanine, β-alanine has no stereocenter.

<span class="mw-page-title-main">Auxotrophy</span> Inability to synthesize an organic compound required for growth

Auxotrophy is the inability of an organism to synthesize a particular organic compound required for its growth. An auxotroph is an organism that displays this characteristic; auxotrophic is the corresponding adjective. Auxotrophy is the opposite of prototrophy, which is characterized by the ability to synthesize all the compounds needed for growth.

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

<span class="mw-page-title-main">Histidine decarboxylase</span> Enzyme that converts histidine to histamine

The enzyme histidine decarboxylase is transcribed on chromosome 15, region q21.1-21.2, and catalyzes the decarboxylation of histidine to form histamine. In mammals, histamine is an important biogenic amine with regulatory roles in neurotransmission, gastric acid secretion and immune response. Histidine decarboxylase is the sole member of the histamine synthesis pathway, producing histamine in a one-step reaction. Histamine cannot be generated by any other known enzyme. HDC is therefore the primary source of histamine in most mammals and eukaryotes. The enzyme employs a pyridoxal 5'-phosphate (PLP) cofactor, in similarity to many amino acid decarboxylases. Eukaryotes, as well as gram-negative bacteria share a common HDC, while gram-positive bacteria employ an evolutionarily unrelated pyruvoyl-dependent HDC. In humans, histidine decarboxylase is encoded by the HDC gene.

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

Pantetheine is the cysteamine amide analog of pantothenic acid (vitamin B5). The dimer of this compound, pantethine is more commonly known, and is considered to be the most potent form of vitamin B5. Pantetheine is an intermediate in the catabolism of coenzyme A by the body.

<span class="mw-page-title-main">Malonyl-CoA decarboxylase</span> Class of enzymes

Malonyl-CoA decarboxylase, is found in bacteria and humans and has important roles in regulating fatty acid metabolism and food intake, and it is an attractive target for drug discovery. It is an enzyme associated with Malonyl-CoA decarboxylase deficiency. In humans, it is encoded by the MLYCD gene.

<span class="mw-page-title-main">Pyruvate dehydrogenase</span> Class of enzymes

Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate.

<span class="mw-page-title-main">Long-chain-fatty-acid—CoA ligase</span> Class of enzymes

The long chain fatty acyl-CoA ligase is an enzyme of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. The enzyme catalyzes the following reaction,

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

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">Histidinol dehydrogenase</span>

In enzymology, histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Diphosphomevalonate decarboxylase</span> InterPro Family

Diphosphomevalonate decarboxylase (EC 4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction

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).

Dr. Herbert Weissbach NAS NAI AAM is an American biochemist/molecular biologist.

References

  1. ↑ American Men of Science: A Biographical Directory. Bowker. 1949. p. 980.
  2. ↑ "Beverly Marie Guirard Obituary (2006) Austin American-Statesman". Legacy.com. Retrieved 2021-12-11.
  3. 1 2 "Beverly Guirard, a pioneer in a man's world". November 15, 2013.
  4. ↑ Guirard, Beverly Marie; Williams, Roger J (1945). The nutritional role of acetate for lactic acid bacteria (PDF). doi:10.26153/tsw/7735. OCLC   1151355220. Archived from the original on December 11, 2021. Retrieved December 11, 2021.{{cite book}}: CS1 maint: bot: original URL status unknown (link)
  5. ↑ 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.
  6. 1 2 3 "Esmond Emerson Snell: 1914 to 2003: A biographical memoir" (PDF). National Academy of Sciences. Archived (PDF) from the original on 2015-09-12. Retrieved December 11, 2021.
  7. ↑ Cheldelin, VH, Eppright, MA, Snell, EE, Guirard, BM (1942). "Enzymatic liberation of B vitamins from plant and animal tissues" (PDF). The University of Texas Publication. Studies on the vitamin content of tissues II: 15–36.
  8. ↑ Guirard, B. M.; Snell, E. E.; Williams, R. J. (1946). "The nutritional role of acetate for lactic acid bacteria; the response to substances related to acetate". Archives of Biochemistry. 9: 361–379. ISSN   0096-9621. PMID   21023612.
  9. ↑ Guirard, B. M.; Snell, E. E.; Williams, R. J. (1946). "The nutritional role of acetate for lactic acid bacteria; fractionation of extracts of natural materials". Archives of Biochemistry. 9: 381–386. ISSN   0096-9621. PMID   21023613.
  10. ↑ Guirard, Beverly M.; Snell, Esmond E.; Williams, Roger J. (1946-02-01). "Microbiological Determination of Amino Acids. IV. Lysine, Histidine, Arginine, and Valine". Proceedings of the Society for Experimental Biology and Medicine. 61 (2): 158–161. doi:10.3181/00379727-61-15258. ISSN   0037-9727. PMID   21017605. S2CID   38376636.
  11. ↑ Wagner, Robert P.; Guirard, Beverly M. (1948-08-01). "A Gene-Controlled Reaction in Neurospora Involving the Synthesis of Pantothenic Acid". Proceedings of the National Academy of Sciences. 34 (8): 398–402. Bibcode:1948PNAS...34..398W. doi: 10.1073/pnas.34.8.398 . ISSN   0027-8424. PMC   1079130 . PMID   16588819.
  12. ↑ Lipmann, Fritz (1954). "Development of the Acetylation Problem, a Personal Account". Science. 120 (3126): 855–865. Bibcode:1954Sci...120..855L. doi:10.1126/science.120.3126.855. ISSN   0036-8075. JSTOR   1683101. PMID   13216186.
  13. ↑ Lipmann, Fritz (December 11, 1953). "Nobel Lecture" (PDF). Archived (PDF) from the original on 2021-12-11.
  14. ↑ Jencks, William P.; Wolfenden, Richard V. (2000). "Fritz Albert Lipmann. 12 June 1899-24 July 1986". Biographical Memoirs of Fellows of the Royal Society. 46: 335–344. ISSN   0080-4606. JSTOR   770404.
  15. ↑ Lipmann, Fritz; Kaplan, Nathan O.; Novelli, G. David; Tuttle, L. Constance; Guirard, Beverly M. (1947). "Coenzyme for Acetylation, a Pantothenic Acid Derivative". Journal of Biological Chemistry. 167 (3): 869–870. doi: 10.1016/S0021-9258(17)30973-0 . PMID   20287921.
  16. ↑ Lipmann, Fritz.; Kaplan, Nathan O.; Novelli, G. David; Tuttle, L. Constance; Guirard, Beverly M. (September 1950). "Isolation of Coenzyme A". Journal of Biological Chemistry. 186 (1): 235–243. doi: 10.1016/S0021-9258(18)56309-2 . PMID   14778827.
  17. ↑ Semenza, G. (2012-12-02). Selected Topics in the History of Biochemistry: Personal Recollections, Part II. Elsevier. ISBN   978-0-444-59821-9.
  18. ↑ Lipmann, Fritz (1984-06-01). "A long life in times of great upheaval". Annual Review of Biochemistry. 53 (1): 1–34. doi: 10.1146/annurev.bi.53.070184.000245 . ISSN   0066-4154. PMID   6383192.
  19. ↑ Lipmann, Fritz (1953). "On Chemistry and Function of Coenzyme A1". Bacteriological Reviews. 17 (1): 1–16. doi:10.1128/br.17.1.1-16.1953. ISSN   0005-3678. PMC   180754 . PMID   13032008.
  20. ↑ Snell, Esmond E.; Guirard, Beverly M.; Williams, Roger J. (1942). "Occurrence in Natural Productgs of a Physiologically Active Metabolite of Pyridoxine". Journal of Biological Chemistry. 143 (2): 519–530. doi: 10.1016/S0021-9258(18)72641-0 .
  21. ↑ Snell, Esmond E.; Guirard, Beverly M. (1943-02-01). "Some Interrelationships of Pyridoxine, Alanine and Glycine in Their Effect on Certain Lactic Acid Bacteria". Proceedings of the National Academy of Sciences. 29 (2): 66–73. Bibcode:1943PNAS...29...66S. doi: 10.1073/pnas.29.2.66 . ISSN   0027-8424. PMC   1078561 . PMID   16588604.
  22. ↑ Guirard, B. M.; Snell, E. E. (1980-06-25). "Purification and properties of ornithine decarboxylase from Lactobacillus sp. 30a". Journal of Biological Chemistry. 255 (12): 5960–5964. doi: 10.1016/S0021-9258(19)70724-8 . ISSN   0021-9258. PMID   7380847.
  23. ↑ Guirard, B M; Snell, E E (1987-09-01). "Purification and properties of pyridoxal-5'-phosphate-dependent histidine decarboxylases from Klebsiella planticola and Enterobacter aerogenes". Journal of Bacteriology. 169 (9): 3963–3968. doi:10.1128/jb.169.9.3963-3968.1987. PMC   213694 . PMID   3114230.
  24. ↑ Guirard, B M; Tanase, S; Snell, E E (1984-01-01). "Pyridoxal-P dependent bacterial histidine decarboxylase". Progress in Clinical and Biological Research. 144A: 235–244. ISSN   0361-7742. PMID   6728848.
  25. ↑ Rosenthaler, J.; Guirard, B. M.; Chang, G. W.; Snell, E. E. (1965-07-01). "Purification and properties of histidine decarboxylase from Lactobacillus 30a". Proceedings of the National Academy of Sciences. 54 (1): 152–158. Bibcode:1965PNAS...54..152R. doi: 10.1073/pnas.54.1.152 . ISSN   0027-8424. PMC   285813 . PMID   5216347.
  26. ↑ Guirard, Beverly (1973). "The amino acid requirements of microorganisms for growth". In Lechevalier, Hubert A. (ed.). CRC Handbook of Microbiology. CRC Press. ISBN   978-0-87819-580-0.
  27. ↑ Guirard, Beverly M.; Snell, Esmond E. (1971-12-01). "Growth Characteristics of a Pseudomonad Which Utilizes Pyridoxine or Pyridoxamine as a Carbon Source". Journal of Bacteriology. 108 (3): 1318–1321. doi:10.1128/jb.108.3.1318-1321.1971. PMC   247221 . PMID   4945196.
  28. ↑ Guirard, Beverly M.; Ames, Bruce N.; Snell, Esmond E. (1971-10-01). "Salmonella typhimurium Mutants with Alternate Requirements for Vitamin B6 or Isoleucine". Journal of Bacteriology. 108 (1): 359–363. doi:10.1128/jb.108.1.359-363.1971. PMC   247074 . PMID   4941563.
  29. ↑ Guirard, Beverly M. (1958-10-01). "Microbial nutrition". Annual Review of Microbiology. 12 (1): 247–278. doi:10.1146/annurev.mi.12.100158.001335. ISSN   0066-4227. PMID   13595607.
  30. ↑ Foley, G. E.; McCarthy, R. E.; Binns, V. M.; Snell, E. E.; Guirard, B. M.; Kidder, G. W.; Dewey, V. C.; Thayer, P. S. (1958). "A Comparative Study of the Use of Microorganisms in the Screening of Potential Antitumor Agents*". Annals of the New York Academy of Sciences. 76 (3): 413–441. Bibcode:1958NYASA..76..413F. doi:10.1111/j.1749-6632.1958.tb54862.x. ISSN   1749-6632. PMID   13627869. S2CID   34678740.
  31. ↑ Guirard, Beverly M.; Snell, Esmond E. (1964-07-01). "Effect of polyamine structure on growth stimulation and spermine and spermidine content of lactic acid bacteria". Journal of Bacteriology. 88 (1): 72–80. doi:10.1128/jb.88.1.72-80.1964. PMC   277258 . PMID   14197908.
  32. ↑ "Longhorn Catholic 2-1 March 2006 [PDF] | Documents Community Sharing". xdocs.pub. Retrieved 2021-12-11.
  33. ↑ "Our Endowments". Catholic Foundation - Diocese of Austin. Retrieved 2021-12-11.
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