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Literature summary 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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.99.10 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
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 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

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.99.10
-
 Bacillus subtilis
3.5.99.10
-
 Pyrococcus furiosus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.99.10 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (1) Bacillus subtilis
a
3.5.99.10 2-iminopropanoate + H2O = pyruvate + NH3 (2) Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.99.10 2-iminobutanoate + H2O
-
 Bacillus subtilis 2-oxobutanoate + NH3
-
 ?
3.5.99.10 2-iminobutanoate + H2O
-
 Pyrococcus furiosus 2-oxobutanoate + NH3
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 2-iminobutanoate + H2O
-
 Bacillus subtilis 168 2-oxobutanoate + NH3
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Bacillus subtilis pyruvate + NH3
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Pyrococcus furiosus pyruvate + NH3
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 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
-
 ?
3.5.99.10 2-iminopropanoate + H2O
-
 Bacillus subtilis 168 pyruvate + NH3
-
 ?
3.5.99.10 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

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

General Information

EC Number General Information Comment Organism
3.5.99.10 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
3.5.99.10 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