Girish Mahajan (Editor)

L serine ammonia lyase

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EC number
  
4.3.1.17

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

MetaCyc
  
metabolic pathway

In enzymology, a L-serine ammonia-lyase (EC 4.3.1.17) is an enzyme that catalyzes the chemical reaction

L-serine pyruvate + NH3

Hence, this enzyme has one substrate, L-serine, and two products, pyruvate 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-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P5J, 1PWE, 1PWH, and 2IQQ.

References

L-serine ammonia-lyase Wikipedia