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1 Structural studies  





2 References  














L-serine ammonia-lyase







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Srpskohrvatski / српскохрватски
 

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From Wikipedia, the free encyclopedia
 


L-serine ammonia-lyase
Serine dehydratase monomer, Human
Identifiers
EC no.4.3.1.17
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 enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction

L-serine = pyruvate + NH3 (overall reaction)
(1a) L-serine = 2-aminoprop-2-enoate + H2O
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)

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, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies[edit]

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

References[edit]


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  • Retrieved from "https://en.wikipedia.org/w/index.php?title=L-serine_ammonia-lyase&oldid=1230294562"

    Categories: 
    EC 4.3.1
    Pyridoxal phosphate enzymes
    Enzymes of known structure
    Enzyme stubs
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    This page was last edited on 21 June 2024, at 21:47 (UTC).

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