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Literature summary for 4.3.1.17 extracted from

  • Zhao, Z.; Liu, H.
    A quantum mechanical/molecular mechanical study on the catalysis of the pyridoxal 5'-phosphate-dependent enzyme L-serine dehydratase (2008), J. Phys. Chem. B, 112, 13091-13100.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine Rattus norvegicus
-
pyruvate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P09367
-
-

Reaction

Reaction Comment Organism Reaction ID
L-serine = pyruvate + NH3 reaction analysis by ab initio quantum mechanical/molecular mechanical method, the reaction involves a Schiff base formation step and a proton-relaying mechanism involving the phosphate of the cofactor in the beta-hydroxyl-leaving step following sequentially after the elimination of the alpha-proton, leading to a single but sequential alpha,beta-elimination step. The rate-limiting transition state is specifically stabilized by the enzyme environment, catalytic mechanism involving Lys41 in the active site, detailed overview Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
Rattus norvegicus pyruvate + NH3
-
?
L-serine alpha,beta-elimination Rattus norvegicus pyruvate + NH3
-
?

Synonyms

Synonyms Comment Organism
L-serine dehydratase
-
Rattus norvegicus
SDH
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Rattus norvegicus