Related Research Articles
Fritz Albert Lipmann was a German-American biochemist and a co-discoverer in 1945 of coenzyme A. For this, together with other research on coenzyme A, he was awarded the Nobel Prize in Physiology or Medicine in 1953.
Günter Wächtershäuser is a German chemist turned patent lawyer who is widely known for his work on the origin of life, and in particular his iron-sulfur world theory, a theory that life on Earth has hydrothermal origins. The hypothesis proposes that early life may have formed on the surface of iron sulfide minerals, hence the name. It was developed by retrodiction from extant biochemistry in conjunction with chemical experiments. The theory is consistent with the hypothesis that life originated near seafloor hydrothermal vents. He was encouraged and supported by science philosopher Karl R. Popper to publish his ideas.
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.
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.
Feodor Felix Konrad Lynen was a German biochemist. In 1964 he won the Nobel Prize in Physiology or Medicine together with Konrad Bloch for their discoveries concerning the mechanism and regulation of cholesterol and fatty acid metabolism while he was director of the Max-Planck Institute for Cellular Chemistry in Munich.
Methionine synthase (MS, MeSe, MTR) is primarily responsible for the regeneration of methionine from homocysteine in most individuals. In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle. There are two primary forms of this enzyme, the Vitamin B12 (cobalamin)-dependent (MetH) and independent (MetE) forms, although minimal core methionine synthases that do not fit cleanly into either category have also been described in some anaerobic bacteria. The two dominant forms of the enzymes appear to be evolutionary independent and rely on considerably different chemical mechanisms. Mammals and other higher eukaryotes express only the cobalamin-dependent form. In contrast, the distribution of the two forms in Archaeplastida (plants and algae) is more complex. Plants exclusively possess the cobalamin-independent form, while algae have either one of the two, depending on species. Many different microorganisms express both the cobalamin-dependent and cobalamin-independent forms.
Methylcobalamin (mecobalamin, MeCbl, or MeB12) is a cobalamin, a form of vitamin B12. It differs from cyanocobalamin in that the cyano group at the cobalt is replaced with a methyl group. Methylcobalamin features an octahedral cobalt(III) centre and can be obtained as bright red crystals. From the perspective of coordination chemistry, methylcobalamin is notable as a rare example of a compound that contains metal–alkyl bonds. Nickel–methyl intermediates have been proposed for the final step of methanogenesis.
Methylmalonyl-CoA mutase (EC 5.4.99.2, MCM), mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MUT gene. This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans. Mutations in MUT gene may lead to various types of methylmalonic aciduria.
Vitamin B12, also known as cobalamin, is a water-soluble vitamin involved in metabolism. It is one of eight B vitamins. It is required by animals, which use it as a cofactor in DNA synthesis, and in both fatty acid and amino acid metabolism. It is important in the normal functioning of the nervous system via its role in the synthesis of myelin, and in the circulatory system in the maturation of red blood cells in the bone marrow. Plants do not need cobalamin and carry out the reactions with enzymes that are not dependent on it.
Cyanocobalamin is a form of vitamin B
12 used to treat and prevent vitamin B
12 deficiency except in the presence of cyanide toxicity. The deficiency may occur in pernicious anemia, following surgical removal of the stomach, with fish tapeworm, or due to bowel cancer. It is used by mouth, by injection into a muscle, or as a nasal spray.
Horace Albert "Nook" Barker (November 29, 1907 – December 24, 2000) was an American biochemist and microbiologist who studied the operation of biological and chemical processes in plants, humans and other animals, including using radioactive tracers to determine the role enzymes play in synthesizing sucrose. He was recognized with the National Medal of Science for his role in identifying an active form of Vitamin B12.
Henry A. Lardy NAS AAA&S APS was a biochemist and professor emeritus in the biochemistry department at the University of Wisconsin-Madison. He was elected to the National Academy of Sciences in 1958, the American Academy of Arts and Sciences in 1965, and the American Philosophical Society in 1976. Research in Lardy's laboratory centered on elucidating the mechanisms underlying metabolism.
Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.
Mary Ellen Jones was an American biochemist. She was notable for discovery of carbamoyl phosphate, a chemical substance that is key to the biosynthesis of arginine and urea, and for the biosynthesis of pyrimidine nucleotides. Jones became the first woman to hold a chair at the University of North Carolina at Chapel Hill, and the first woman to become a department chair at the medical school. She was a member of the National Academy of Sciences. She was also president of the Association of Medical School Departments of Biochemistry, president of the American Society for Biochemistry and Molecular Biology, and president of the American Association of University Professors. The New York Times called her a "crucial researcher on DNA" and said that her studies laid the foundation for basic cancer research. She died of cancer on August 23, 1996.
Rowena Green Matthews 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.
Malcolm Daniel Lane was a biochemist who spent most of his career on the faculty at the Johns Hopkins School of Medicine in Baltimore, Maryland. Lane served as the head of the Department of Biological Chemistry from 1978 to 1997, was elected to the National Academy of Sciences in 1987, and was named a University Distinguished Service Professor – the institution's highest academic title – in 2001. Lane's research focused on the biochemistry of lipids and lipid metabolism, and the resulting physiological mechanisms regulating adipogenesis and obesity.
Dr. Herbert Weissbach NAS NAI AAM is an American biochemist/molecular biologist.
Ruma Banerjee is a professor of enzymology and biological chemistry at the University of Michigan Medical School. She is an experimentalist whose research has focused on unusual cofactors in enzymology.
Cobalt is essential to the metabolism of all animals. It is a key constituent of cobalamin, also known as vitamin B12, the primary biological reservoir of cobalt as an ultratrace element. Bacteria in the stomachs of ruminant animals convert cobalt salts into vitamin B12, a compound which can only be produced by bacteria or archaea. A minimal presence of cobalt in soils therefore markedly improves the health of grazing animals, and an uptake of 0.20 mg/kg a day is recommended because they have no other source of vitamin B12.
References
- ↑ Who's who in the South and Southwest. October 1984. ISBN 9780837908199.
- 1 2 3 "Richard Wolfenden Faculty Page". Department of Chemistry/UNC Chapel Hill. Retrieved 30 December 2009.
- ↑ "Richard Wolfenden, Biochemistry and Biophysics". The University of North Carolina at Chapel Hill School of Medicine. 2009. Retrieved 30 December 2009.
- ↑ Taylor, Edith (May 1, 2002). "National Academy of Sciences Elects New Members and Associates". The Chronicle of Higher Education. Retrieved 30 December 2009.
- 1 2 Lynch, Brendan (2 September 2009). "Celebrated researcher Richard Wolfenden to explain how enzymes make life thrive". The University of Kansas. Retrieved 30 December 2009.
- ↑ "Enzyme importance reinforced". Scientist Live, Setform Limited. 2008. Retrieved 30 December 2009.
- ↑ Wolfenden, Richard Vance (1956). "Metabolism of Cobalt and Vitamin B12 in Rats".
- ↑ "Celebrated researcher Richard Wolfenden to explain how enzymes make life thrive - KU News". archive.news.ku.edu. Retrieved 2020-06-19.
- ↑ "Richard Vance Wolfenden". American Academy of Arts & Sciences. Retrieved 2020-06-19.
