Aspartate ammonia-lyase

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aspartate ammonia-lyase
Identifiers
EC number4.3.1.1
CAS number9027-30-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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. 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[edit]

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

References[edit]

  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.CS1 maint: uses authors parameter (link)
  • Ellfolk N, Kjærgård T, Bánhidi ZG, Virtanen AI, Sörensen NA (1953). "Studies on aspartase. 1. Quantitative separation of aspartase from bacterial cells, and its partial purification". Acta Chem. Scand. 7: 824–830. doi:10.3891/acta.chem.scand.07-0824.