D-threonine aldolase
| D-threonine aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 glycine + acetaldehyde
- (2) D-allothreonine glycine + acetaldehyde
This pyridoxal-phosphate protein is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+).
References
- ^ Kataoka, M., Ikemi, M., Morikawa, T., Miyoshi, T., Nishi, K., Wada, M., Yamada, H. and Shimizu, S. (1997). "Isolation and characterization of D-threonine aldolase, a pyridoxal-5′-phosphate-dependent enzyme from Arthrobacter sp. DK-38". Eur. J. Biochem. 248: 385–393. doi:10.1111/j.1432-1033.1997.00385.x. PMID 9346293.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (1998). "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". J. Biol. Chem. 273: 16678–16685. doi:10.1074/jbc.273.27.16678. PMID 9642221.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Liu, J.Q., Odani, M., Dairi, T., Itoh, N., Shimizu, S. and Yamada, H. (1999). "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". Appl. Microbiol. Biotechnol. 51: 586–591. doi:10.1007/s002530051436. PMID 10390816.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Liu, J.Q., Odani, M., Yasuoka, T., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (2000). "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". Appl. Microbiol. Biotechnol. 54: 44–51. doi:10.1007/s002539900301. PMID 10952004.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (2000). "Diversity of microbial threonine aldolases and their application". J. Mol. Catal. B. 10: 107–115. doi:10.1016/s1381-1177(00)00118-1.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Paiardini, A., Contestabile, R., D'Aguanno, S., Pascarella, S. and Bossa, F. (2003). "Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes". Biochim. Biophys. Acta. 1647: 214–219. doi:10.1016/s1570-9639(03)00050-5. PMID 12686135.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- D-threonine+aldolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)