Aspartate ammonia-lyase

From Wikipedia, the free encyclopedia

In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction

L-aspartate fumarate + NH₃

Hence, this enzyme has one substrate, L-aspartate, and two products, fumarate and NH₃.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism.

Contents 1 Structural studies 2 References 3 External links 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J3U and 1JSW.

[edit] References

• IUBMB entry for 4.3.1.1
• BRENDA references for 4.3.1.1 (Recommended.)
• PubMed references for 4.3.1.1
• PubMed Central references for 4.3.1.1
• Google Scholar references for 4.3.1.1
• Ellfolk N (1953). "Studies on aspartase. 1. Quantitative separation of aspartase from bacterial cells, and its partial purification". Acta Chem. Scand. 7: 824–830. 

[edit] External links

The CAS registry number for this enzyme class is 9027-30-9.

• IUBMB entry for 4.3.1.1

• KEGG entry for 4.3.1.1

• BRENDA entry for 4.3.1.1

• NiceZyme view of 4.3.1.1

• EC2PDB: PDB structures for 4.3.1.1

• PRIAM entry for 4.3.1.1

• PUMA2 entry for 4.3.1.1

• IntEnz: Integrated Enzyme entry for 4.3.1.1

• MetaCyc entry for 4.3.1.1

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0008797: aspartate ammonia-lyase

• AMIGO entry for GO code 0008797: aspartate ammonia-lyase