D-serine ammonia-lyase

D-serine ammonia-lyase
Identifiers
EC number	4.3.1.18
CAS number	9015-88-7
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, a D-serine ammonia-lyase (EC 4.3.1.18) is an enzyme that catalyzes the chemical reaction

D-serine $\rightleftharpoons$ pyruvate + NH₃

Hence, this enzyme has one substrate, D- in common use include D-hydroxyaminoacid dehydratase, D-serine dehydrase, D-hydroxy amino acid dehydratase, D-serine hydrolase, D-serine dehydratase (deaminating), D-serine deaminase, and D-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

References

• Dupourque D, Newton WA, Snell EE (1966). "Purification and properties of D-serine dehydrase from Escherichia coli". J. Biol. Chem. 241 (5): 1233–8. PMID 5327100. 
• METZLER DE, SNELL EE (1952). "Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme from Escherichia coli". J. Biol. Chem. 198 (1): 363–73. PMID 12999751. 

This lyase article is a stub. You can help Wikipedia by expanding it.v · Categories: EC 4.3.1 Pyridoxal phosphate enzymes Enzymes of unknown structure Lyase stubs Wikimedia Foundation. 2010. Игры ⚽ Поможем написать реферат Rondo Hatton Classic Horror Awards Erythro-3-hydroxyaspartate ammonia-lyase Look at other dictionaries: Carbamoyl-serine ammonia-lyase — In enzymology, a carbamoyl serine ammonia lyase (EC number|4.3.1.13) is an enzyme that catalyzes the chemical reaction:O carbamoyl L serine + H2O ightleftharpoons pyruvate + 2 NH3 + CO2Thus, the two substrates of this enzyme are O carbamoyl L… …   Wikipedia L-serine ammonia-lyase — In enzymology, a L serine ammonia lyase (EC number|4.3.1.17) is an enzyme that catalyzes the chemical reaction:L serine ightleftharpoons pyruvate + NH3Hence, this enzyme has one substrate, L serine, and two products, pyruvate and NH3.This enzyme… …   Wikipedia L-serine ammonia-lyase — L ser·ine am·mo·nia ly·ase (sērґēn ə moґne ə liґās) [EC 4.3.1.17] an enzyme of the lyase class that catalyzes the elimination of ammonia from L serine, with formation of a double bond to yield pyruvate. The enzyme… …   Medical dictionary Serine-sulfate ammonia-lyase — In enzymology, a serine sulfate ammonia lyase (EC number|4.3.1.10) is an enzyme that catalyzes the chemical reaction:L serine O sulfate + H2O ightleftharpoons pyruvate + NH3 + sulfateThus, the two substrates of this enzyme are L serine O sulfate… …   Wikipedia Threonine ammonia-lyase — In enzymology, a threonine ammonia lyase (EC number|4.3.1.19) is an enzyme that catalyzes the chemical reaction:L threonine ightleftharpoons 2 oxobutanoate + NH3Hence, this enzyme has one substrate, L threonine, and two products, 2 oxobutanoate… …   Wikipedia L-serine dehydratase — L ser·ine de·hy·dra·tase (sērґēn de hiґdrə tās) former official name for L serine ammonia lyase …   Medical dictionary Serine — Not to be confused with Sarin. Serine …   Wikipedia Cystathionine gamma-lyase — Cysteine metabolism. Cystathionase catalyzes the lower reaction. Identifiers EC number …   Wikipedia 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 Amino acid — This article is about the class of chemicals. For the structures and properties of the standard proteinogenic amino acids, see Proteinogenic amino acid. The generic structure of an alpha amino acid in its unionized form …   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”