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Literature summary for 3.5.99.10 extracted from

  • Lambrecht, J.A.; Flynn, J.M.; Downs, D.M.
    Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme reactions (2012), J. Biol. Chem., 287, 3454-3461.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.99.10

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-iminobutanoate + H2O Bacillus subtilis the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O Pyrococcus furiosus the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O Bacillus subtilis 168 the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates 2-oxobutanoate + NH3
-
 ?
2-iminopropanoate + H2O Bacillus subtilis the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates pyruvate + NH3
-
 ?
2-iminopropanoate + H2O Pyrococcus furiosus the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates pyruvate + NH3
-
 ?
2-iminopropanoate + H2O Bacillus subtilis 168 the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates pyruvate + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P37552
-
-
Bacillus subtilis 168 P37552
-
-
Pyrococcus furiosus Q8U308
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis
-
 Pyrococcus furiosus

Reaction

Reaction Comment Organism Reaction ID
2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (1) Bacillus subtilis
a
2-iminopropanoate + H2O = pyruvate + NH3 (2) Bacillus subtilis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-iminobutanoate + H2O
-
 Bacillus subtilis 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O
-
 Pyrococcus furiosus 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Bacillus subtilis 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Pyrococcus furiosus 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O
-
 Bacillus subtilis 168 2-oxobutanoate + NH3
-
 ?
2-iminobutanoate + H2O the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Bacillus subtilis 168 2-oxobutanoate + NH3
-
 ?
2-iminopropanoate + H2O
-
 Bacillus subtilis pyruvate + NH3
-
 ?
2-iminopropanoate + H2O
-
 Pyrococcus furiosus pyruvate + NH3
-
 ?
2-iminopropanoate + H2O the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Bacillus subtilis pyruvate + NH3
-
 ?
2-iminopropanoate + H2O the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Pyrococcus furiosus pyruvate + NH3
-
 ?
2-iminopropanoate + H2O
-
 Bacillus subtilis 168 pyruvate + NH3
-
 ?
2-iminopropanoate + H2O the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Bacillus subtilis 168 pyruvate + NH3
-
 ?

Synonyms

Synonyms Comment Organism
enamine/imine deaminase ambiguous Bacillus subtilis
enamine/imine deaminase ambiguous Pyrococcus furiosus
ridA
-
 Bacillus subtilis
ridA
-
 Pyrococcus furiosus
yjgF
-
 Bacillus subtilis
yjgF
-
 Pyrococcus furiosus

General Information

General Information Comment Organism
physiological function the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Bacillus subtilis
physiological function the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates Pyrococcus furiosus