"Cysteine Synthase" 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.
An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.
| Descriptor ID |
D003547
|
| MeSH Number(s) |
D08.811.913.225.224
|
| Concept/Terms |
Cysteine Synthase- Cysteine Synthase
- O-Acetylserine Sulfhydrylase
- O Acetylserine Sulfhydrylase
- Sulfhydrylase, O-Acetylserine
- O-Acetylserine (Thiol)-Lyase
|
Below are MeSH descriptors whose meaning is more general than "Cysteine Synthase".
Below are MeSH descriptors whose meaning is more specific than "Cysteine Synthase".
This graph shows the total number of publications written about "Cysteine Synthase" by people in this website by year, and whether "Cysteine Synthase" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1993 | 2 | 0 | 2 |
| 1994 | 1 | 0 | 1 |
| 1995 | 3 | 0 | 3 |
| 1996 | 5 | 0 | 5 |
| 1997 | 1 | 0 | 1 |
| 1998 | 3 | 0 | 3 |
| 1999 | 2 | 0 | 2 |
| 2000 | 2 | 0 | 2 |
| 2001 | 2 | 0 | 2 |
| 2002 | 1 | 0 | 1 |
| 2003 | 3 | 0 | 3 |
| 2004 | 1 | 0 | 1 |
| 2005 | 2 | 0 | 2 |
| 2006 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2008 | 2 | 0 | 2 |
| 2009 | 1 | 0 | 1 |
| 2010 | 3 | 0 | 3 |
| 2011 | 1 | 0 | 1 |
| 2012 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
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Below are the most recent publications written about "Cysteine Synthase" by people in Profiles.
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Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target. PLoS One. 2013; 8(10):e77558.
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Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase. Biochim Biophys Acta. 2013 Jan; 1834(1):169-81.
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The multifaceted pyridoxal 5'-phosphate-dependent O-acetylserine sulfhydrylase. Biochim Biophys Acta. 2011 Nov; 1814(11):1497-510.
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Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A. Biochemistry. 2010 Jul 27; 49(29):6093-103.
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A two-step process controls the formation of the bienzyme cysteine synthase complex. J Biol Chem. 2010 Apr 23; 285(17):12813-22.
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Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. J Med Chem. 2010 Jan 14; 53(1):345-56.
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(31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Arch Biochem Biophys. 2009 Jul 15; 487(2):85-90.
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Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction. Arch Biochem Biophys. 2008 Apr 15; 472(2):115-25.
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Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. Biochim Biophys Acta. 2008 Apr; 1784(4):629-37.
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Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry. 2007 Jul 17; 46(28):8315-30.