Oxalomalate lyase

oxalomalate lyase
Identifiers
EC number	4.1.3.13
CAS number	37290-63-4
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
Search PMC articles PubMed articles

In enzymology, an oxalomalate lyase (EC 4.1.3.13) is an enzyme that catalyzes the chemical reaction

3-oxalomalate $\rightleftharpoons$ oxaloacetate + glyoxylate

Hence, this enzyme has one substrate, 3-oxalomalate, and two products, oxaloacetate and glyoxylate.

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-oxalomalate glyoxylate-lyase (oxaloacetate-forming). This enzyme is also called 3-oxalomalate glyoxylate-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

References

• Sekizawa Y, Maragoudakis ME, King TE, Cheldelin VH (1966). "Glutamate biosynthesis in an organism lacking a Krebs tricarboxylic acid cycle. V. Isolation of alpha-hydroxy-gamma-ketoglutarate (HKG) in Acetobacter suboxydans". Biochemistry. 5 (7): 2392–8. doi:10.1021/bi00871a032. PMID 6005666. 

This EC 4.1 enzyme-related article is a stub. You can help Wikipedia by expanding it.v · Categories: EC 4.1 stubs EC 4.1.3 Enzymes of unknown structure Wikimedia Foundation. 2010. Игры ⚽ Поможем написать реферат Oxalate decarboxylase Coagulation factor II receptor Look at other dictionaries: List of EC numbers (EC 4) — This list contains a list of EC numbers for the fourth group, EC 4, lyases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 4.1: Carbon Carbon LyasesEC… …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”