Biology:D-threonine aldolase
From HandWiki
| D-threonine aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.2.42 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
D-threonine aldolase (EC 4.1.2.42, D-TA, DTA, low specificity D-TA, low specificity D-threonine aldolase) is an enzyme with systematic name D-threonine acetaldehyde-lyase (glycine-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- (1) D-threonine [math]\displaystyle{ \rightleftharpoons }[/math] glycine + acetaldehyde
- (2) D-allothreonine [math]\displaystyle{ \rightleftharpoons }[/math] glycine + acetaldehyde
This pyridoxal-phosphate protein is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+).
References
- ↑ "Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38". European Journal of Biochemistry 248 (2): 385–93. September 1997. doi:10.1111/j.1432-1033.1997.00385.x. PMID 9346293.
- ↑ "A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization". The Journal of Biological Chemistry 273 (27): 16678–85. July 1998. doi:10.1074/jbc.273.27.16678. PMID 9642221.
- ↑ "A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution". Applied Microbiology and Biotechnology 51 (5): 586–91. May 1999. doi:10.1007/s002530051436. PMID 10390816.
- ↑ "Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug". Applied Microbiology and Biotechnology 54 (1): 44–51. July 2000. doi:10.1007/s002539900301. PMID 10952004.
- ↑ Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H. (2000). "Diversity of microbial threonine aldolases and their application". J. Mol. Catal. B 10 (1–3): 107–115. doi:10.1016/s1381-1177(00)00118-1.
- ↑ "Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1647 (1–2): 214–9. April 2003. doi:10.1016/s1570-9639(03)00050-5. PMID 12686135.
External links
- D-threonine+aldolase at the US National Library of Medicine Medical Subject Headings (MeSH)
 |  |
