Aspartate 4-decarboxylase

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aspartate 4-decarboxylase
3fdd.jpg
Aspartate beta-decarboxylase dodekamer, Comamonas testosteroni
Identifiers
EC number4.1.1.12
CAS number9024-57-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction

L-aspartate L-alanine + CO2

Hence, this enzyme has one substrate, L-aspartate, and two products, L-alanine and CO2. This reaction is the basis of the industrial synthesis of L-alanine.[1]

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-aspartate 4-carboxy-lyase (L-alanine-forming). Other names in common use include desulfinase, aminomalonic decarboxylase, aspartate beta-decarboxylase, aspartate omega-decarboxylase, aspartic omega-decarboxylase, aspartic beta-decarboxylase, L-aspartate beta-decarboxylase, cysteine sulfinic desulfinase, L-cysteine sulfinate acid desulfinase, and L-aspartate 4-carboxy-lyase. This enzyme participates in alanine and aspartate metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

References[edit]

  1. ^ Karlheinz Drauz, Ian Grayson, Axel Kleemann, Hans-Peter Krimmer, Wolfgang Leuchtenberger, Christoph Weckbecker (2006). Ullmann's Encyclopedia of Industrial Chemistry. Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2.CS1 maint: Multiple names: authors list (link)
  • Kakimoto T, Kato J, Shibatani T, Nishimura N, Chibata I (1969). "Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae I. Crystallization and some physiocochemical properties". J. Biol. Chem. 244 (2): 353–8. PMID 5773301.
  • Novogrodsky A; Meister A (1964). "Control of aspartate beta-decarboxylase activity by transamination". J. Biol. Chem. 239: 879–888. PMID 14154469.
  • Palekar AG, Tate SS, Meister A (1970). "Inhibition of aspartate beta-decarboxylase by aminomalonate Stereospecific decarboxylation of aminomalonate to glycine". Biochemistry. 9 (11): 2310–5. doi:10.1021/bi00813a014. PMID 5424207.
  • Wilson EM; Kornberg HL (1963). "Properties of crystalline l-aspartate 4-carboxy-lyase from Achromobacter sp". Biochem. J. 88 (3): 578–587. PMC 1202217. PMID 14071532.