Aspartate ammonia-lyase

The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction

L-aspartate fumarate + NH3
aspartate ammonia-lyase
Aspartate ammonia-lyase homotetramer, Bacillus sp. YM55-1
Identifiers
EC no.4.3.1.1
CAS no.9027-30-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The reaction is the basis of the industrial synthesis of aspartate.[1]

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.

Structural studies

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

References

  1. Karlheinz Drauz; Ian Grayson; Axel Kleemann; Hans-Peter Krimmer; Wolfgang Leuchtenberger; Christoph Weckbecker (2006). "Amino Acids". Ullmann's Encyclopedia of Industrial Chemistry. Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2.


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