"Carboxy-Lyases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
| Descriptor ID |
D002262
|
| MeSH Number(s) |
D08.811.520.224.125
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Carboxy-Lyases".
Below are MeSH descriptors whose meaning is more specific than "Carboxy-Lyases".
This graph shows the total number of publications written about "Carboxy-Lyases" by people in this website by year, and whether "Carboxy-Lyases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2003 | 1 | 1 | 2 |
| 2004 | 1 | 0 | 1 |
| 2005 | 2 | 0 | 2 |
| 2010 | 0 | 1 | 1 |
| 2011 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2016 | 0 | 1 | 1 |
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Below are the most recent publications written about "Carboxy-Lyases" by people in Profiles.
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Johnson WH, Stack TM, Taylor SM, Burks EA, Whitman CP. Stereochemical Consequences of Vinylpyruvate Hydratase-Catalyzed Reactions. Biochemistry. 2016 07 26; 55(29):4055-64.
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Guo Y, Serrano H, Poelarends GJ, Johnson WH, Hackert ML, Whitman CP. Kinetic, mutational, and structural analysis of malonate semialdehyde decarboxylase from Coryneform bacterium strain FG41: mechanistic implications for the decarboxylase and hydratase activities. Biochemistry. 2013 Jul 16; 52(28):4830-41.
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Balakrishnan A, Paramasivam S, Chakraborty S, Polenova T, Jordan F. Solid-state nuclear magnetic resonance studies delineate the role of the protein in activation of both aromatic rings of thiamin. J Am Chem Soc. 2012 Jan 11; 134(1):665-72.
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Whitaker WB, Parent MA, Naughton LM, Richards GP, Blumerman SL, Boyd EF. Modulation of responses of Vibrio parahaemolyticus O3:K6 to pH and temperature stresses by growth at different salt concentrations. Appl Environ Microbiol. 2010 Jul; 76(14):4720-9.
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Almrud JJ, Poelarends GJ, Johnson WH, Serrano H, Hackert ML, Whitman CP. Crystal structures of the wild-type, P1A mutant, and inactivated malonate semialdehyde decarboxylase: a structural basis for the decarboxylase and hydratase activities. Biochemistry. 2005 Nov 15; 44(45):14818-27.
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Poelarends GJ, Serrano H, Johnson WH, Whitman CP. Inactivation of malonate semialdehyde decarboxylase by 3-halopropiolates: evidence for hydratase activity. Biochemistry. 2005 Jul 05; 44(26):9375-81.
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Poelarends GJ, Serrano H, Johnson WH, Hoffman DW, Whitman CP. The hydratase activity of malonate semialdehyde decarboxylase: mechanistic and evolutionary implications. J Am Chem Soc. 2004 Dec 08; 126(48):15658-9.
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Tomas CA, Welker NE, Papoutsakis ET. Overexpression of groESL in Clostridium acetobutylicum results in increased solvent production and tolerance, prolonged metabolism, and changes in the cell's transcriptional program. Appl Environ Microbiol. 2003 Aug; 69(8):4951-65.
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Tummala SB, Welker NE, Papoutsakis ET. Design of antisense RNA constructs for downregulation of the acetone formation pathway of Clostridium acetobutylicum. J Bacteriol. 2003 Mar; 185(6):1923-34.
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Herrera-Ornelas L, Porter C, Pera P, Greco W, Petrelli NJ, Mittelman A. A comparison of ornithine decarboxylase and S-adenosylmethionine decarboxylase activity in human large bowel mucosa, polyps, and colorectal adenocarcinoma. J Surg Res. 1987 Jan; 42(1):56-60.