Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | homologues of substrate D-lysine, D-2,5-diaminopentanoic acid, 2,4-diaminobutyric acid, and D-2,3-diaminopropionic acid bind to pyridoxal 5'-phosphate as an external aldimine and elicit the 5'-deoxyadenosylcobalamin Co-C bond homolysis and the accumulations of cob(II)alamin and analogue-based radicals. The position for hydrogen atom abstraction from D-2,5-diaminopentanoic acid and 2,4-diaminobutyric acid by the 5'-deoxyadenosyl radical occurs at the carbon adjacent to the imine, resulting in overstabilized radicals by spin delocalization through the imine into the pyridine ring of pyridoxal 5'-phosphate. These radicals block the active site, inhibit the enzyme, and poise the enzyme into two distinct conformations: for even-numbered analogues, the cob(II)alamin remains proximal to and spin-coupled with the analogue-based radical in the closed state while odd-numbered analogues trigger the transition to the open state of the enzyme, inactivation mechanism, overview | Acetoanaerobium sticklandii | |
additional information | homologues of substrate D-lysine, D-2,5-diaminopentanoic acid, 2,4-diaminobutyric acid, and D-2,3-diaminopropionic acid bind to pyridoxal 5'-phosphate as an external aldimine and elicit the 5'-deoxyadenosylcobalamin Co-C bond homolysis and the accumulations of cob(II)alamin and analogue-based radicals. The position for hydrogen atom abstraction from D-2,5-diaminopentanoic acid and 2,4-diaminobutyric acid by the 5'-deoxyadenosyl radical occurs at the carbon adjacent to the imine, resulting in overstabilized radicals by spin delocalization through the imine into the pyridine ring of pyridoxal 5'-phosphate. These radicals block the active site, inhibit the enzyme, and poise the enzyme into two distinct conformations: for even-numbered analogues, the cob(II)alamin remains proximal to and spin-coupled with the analogue-based radical in the closed state while odd-numbered analogues trigger the transition to the open state of the enzyme, inactivation mechanism, overview | Propionibacterium freudenreichii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(3S)-3,6-diaminohexanoate | Acetoanaerobium sticklandii | - |
(3S,5S)-3,5-diaminohexanoate | - |
r | |
(3S)-3,6-diaminohexanoate | Propionibacterium freudenreichii | - |
(3S,5S)-3,5-diaminohexanoate | - |
r | |
(3S)-3,6-diaminohexanoate | Propionibacterium freudenreichii ATCC 9614 | - |
(3S,5S)-3,5-diaminohexanoate | - |
r | |
(3S)-3,6-diaminohexanoate | Acetoanaerobium sticklandii StadtmanHF | - |
(3S,5S)-3,5-diaminohexanoate | - |
r | |
D-lysine | Acetoanaerobium sticklandii | - |
2,5-diaminohexanoate | - |
r | |
D-lysine | Propionibacterium freudenreichii | - |
2,5-diaminohexanoate | - |
r | |
D-lysine | Propionibacterium freudenreichii ATCC 9614 | - |
2,5-diaminohexanoate | - |
r | |
D-lysine | Acetoanaerobium sticklandii StadtmanHF | - |
2,5-diaminohexanoate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acetoanaerobium sticklandii | - |
- |
- |
Acetoanaerobium sticklandii StadtmanHF | - |
- |
- |
Propionibacterium freudenreichii | - |
subsp. shermanii | - |
Propionibacterium freudenreichii ATCC 9614 | - |
subsp. shermanii | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate | catalytic mechanism, the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Acetoanaerobium sticklandii | |
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate | catalytic mechanism, the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Propionibacterium freudenreichii | |
D-lysine = (2R,5S)-2,5-diaminohexanoate | catalytic mechanism, the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Acetoanaerobium sticklandii | |
D-lysine = (2R,5S)-2,5-diaminohexanoate | catalytic mechanism, the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Propionibacterium freudenreichii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(3S)-3,6-diaminohexanoate | - |
Acetoanaerobium sticklandii | (3S,5S)-3,5-diaminohexanoate | - |
r | |
(3S)-3,6-diaminohexanoate | - |
Propionibacterium freudenreichii | (3S,5S)-3,5-diaminohexanoate | - |
r | |
(3S)-3,6-diaminohexanoate | - |
Propionibacterium freudenreichii ATCC 9614 | (3S,5S)-3,5-diaminohexanoate | - |
r | |
(3S)-3,6-diaminohexanoate | - |
Acetoanaerobium sticklandii StadtmanHF | (3S,5S)-3,5-diaminohexanoate | - |
r | |
D-lysine | - |
Acetoanaerobium sticklandii | 2,5-diaminohexanoate | - |
r | |
D-lysine | - |
Propionibacterium freudenreichii | 2,5-diaminohexanoate | - |
r | |
D-lysine | - |
Propionibacterium freudenreichii ATCC 9614 | 2,5-diaminohexanoate | - |
r | |
D-lysine | - |
Acetoanaerobium sticklandii StadtmanHF | 2,5-diaminohexanoate | - |
r | |
additional information | the enzyme can accept D-lysine and L-beta-lysine | Acetoanaerobium sticklandii | ? | - |
? | |
additional information | the enzyme can accept D-lysine and L-beta-lysine | Propionibacterium freudenreichii | ? | - |
? | |
additional information | the enzyme can accept D-lysine and L-beta-lysine | Propionibacterium freudenreichii ATCC 9614 | ? | - |
? | |
additional information | the enzyme can accept D-lysine and L-beta-lysine | Acetoanaerobium sticklandii StadtmanHF | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
5,6-LAM | - |
Acetoanaerobium sticklandii |
5,6-LAM | - |
Propionibacterium freudenreichii |
lysine 5,6-aminomutase | - |
Acetoanaerobium sticklandii |
lysine 5,6-aminomutase | - |
Propionibacterium freudenreichii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5'-deoxyadenosylcobalamin | dependent on | Acetoanaerobium sticklandii | |
5'-deoxyadenosylcobalamin | dependent on | Propionibacterium freudenreichii | |
additional information | the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Acetoanaerobium sticklandii | |
additional information | the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Propionibacterium freudenreichii | |
additional information | the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal-5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Propionibacterium freudenreichii | |
pyridoxal 5'-phosphate | dependent on | Acetoanaerobium sticklandii | |
pyridoxal 5'-phosphate | dependent on | Propionibacterium freudenreichii |
General Information | Comment | Organism |
---|---|---|
additional information | the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Acetoanaerobium sticklandii |
additional information | the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine | Propionibacterium freudenreichii |