Tagatose-bisphosphate aldolase
tagatose-bisphosphate aldolase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 4.1.2.40 | ||||||||
CAS number | 39433-95-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
|
In enzymology, a tagatose-bisphosphate aldolase (EC 4.1.2.40) is an enzyme that catalyzes the chemical reaction
- D-tagatose 1,6-bisphosphate glycerone phosphate + D-glyceraldehyde 3-phosphate
Hence, this enzyme has one substrate, D-tagatose 1,6-bisphosphate, and two products, glycerone phosphate and D-glyceraldehyde 3-phosphate.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is D-tagatose 1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming). This enzyme is also called D-tagatose-1,6-bisphosphate triosephosphate lyase. This enzyme participates in galactose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1GVF.
References
- Anderson RL, Markwell JP (1982). "D-Tagatose-1,6-bisphosphate aldolase (Class II) from Klebsiella pneumoniae". Methods Enzymol. 90: 323–324. doi:10.1016/s0076-6879(82)90131-8. PMID 6759854.
- van Rooijen RJ, van Schalkwijk S, de Vos WM (1991). "Molecular cloning, characterization, and nucleotide sequence of the tagatose 6-phosphate pathway gene cluster of the lactose operon of Lactococcus lactis". J. Biol. Chem. 266 (11): 7176–81. PMID 1901863.
This article is issued from Wikipedia - version of the 5/23/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.