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Information on EC 4.3.1.17 - L-serine ammonia-lyase

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.17 L-serine ammonia-lyase
IUBMB Comments
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead . The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. This reaction is also carried out by EC 4.3.1.19, threonine ammonia-lyase, from a number of sources.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
serine dehydratase, l-threonine deaminase, l-threonine dehydratase, l-serine deaminase, serdh, serine deaminase, lplsd, l-sd2, msmeg_3532, l-sd1, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
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(1b), spontaneous
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2-iminopropanoate + H2O = pyruvate + NH3
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(1c), spontaneous
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L-serine = 2-aminoprop-2-enoate + H2O
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(1a)
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L-serine = pyruvate + NH3
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