5.4.3.5: D-ornithine 4,5-aminomutase
This is an abbreviated version!
For detailed information about D-ornithine 4,5-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.5
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5.4.3.5
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pyridoxal
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sticklandii
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adocbl
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homolysis
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5'-phosphate
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plp-dependent
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5,6-aminomutase
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aldimine
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rossmann
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radical-based
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stopped-flow
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5\'-deoxyadenosyl
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paramagnetic
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1,2-amino
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deprotonated
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d-lysine
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cobalamin-binding
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rupture
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ribose
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imine
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interconverting
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5\'-deoxyadenosylcobalamin
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multistep
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adocbl-dependent
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isomerization
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pyridoxal-5'-phosphate
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pyridine
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uv-visible
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refolding
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synergy
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b12-dependent
- 5.4.3.5
- pyridoxal
- sticklandii
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adocbl
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homolysis
- 5'-phosphate
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plp-dependent
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5,6-aminomutase
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aldimine
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rossmann
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radical-based
-
stopped-flow
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5\'-deoxyadenosyl
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paramagnetic
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1,2-amino
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deprotonated
- d-lysine
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cobalamin-binding
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rupture
- ribose
- imine
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interconverting
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5\'-deoxyadenosylcobalamin
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multistep
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adocbl-dependent
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isomerization
- pyridoxal-5'-phosphate
- pyridine
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uv-visible
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refolding
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synergy
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b12-dependent
Reaction
Synonyms
4,5-OAM, adenosylcobalamin-dependent ornithine 4,5-aminomutase, Aminomutase, D-ornithine 4,5-, D-ornithine aminomutase, OAM, oraE, oraS, ornithine 4,5-aminomutase, ornithine aminomutase
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KM Value
KM Value on EC 5.4.3.5 - D-ornithine 4,5-aminomutase
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0.029
pH 8.5, 25°C, recombinant beta-subunit mutant S162A
0.03
D-ornithine
recombinant His-tagged mutant E338A, pH 7.5, 30°C
0.031
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant Y187F
0.043
D-ornithine
pH 8.5, 25°C, recombinant wild-type enzyme
0.043
D-ornithine
recombinant His-tagged mutant E338D, pH 7.5, 30°C
0.061
D-ornithine
recombinant His-tagged mutant E338Q, pH 7.5, 30°C
0.12
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant N226D
0.14
D-ornithine
recombinant mutant H225A, pH 8.5, 25°C
0.14
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant Y160F
0.176
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant E338A
0.185
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant I424E
0.186
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant C700S
0.189
D-ornithine
pH 8.5, 25°C, recombinant wild-type enzyme
0.19
D-ornithine
recombinant His-tagged wild-type enzyme, pH 7.5, 30°C
0.19
D-ornithine
recombinant wild-type, pH 8.5, 25°C
0.19
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant G339W
0.193
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant D627A
0.193
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant P343W
0.2
D-ornithine
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pH and temperature not specified in the publication
0.453
D-ornithine
recombinant mutant H225Q, pH 8.5, 25°C
0.78
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant E81A
0.87
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant E81Q
4.9
D-ornithine
pH 8.5, 25°C, recombinant beta-subunit mutant R297K
0.068
pH 8.5, 20°C, recombinant beta-subunit mutant Y187A
0.162
DL-Ornithine
pH 8.5, 20°C, recombinant beta-subunit mutant Y187F
0.567
DL-Ornithine
pH 8.5, 20°C, recombinant wild-type enzyme
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
pre-steady-state and stedy-state kinetics of wild-type and mutant enzymes
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additional information
additional information
pre-steady-state and stedy-state kinetics of wild-type and mutant enzymes
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additional information
additional information
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pre-steady-state and stedy-state kinetics of wild-type and mutant enzymes
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additional information
additional information
kinetic isotope effects analysis using isotope-labeled DL-ornithine-3,3,4,4,5,5-d6 revealing a diminished Dkcat/Km of 2.5 relative to a Dkcat of 7.6, suggesting slow release of the substrate from the active site. Kinetic isotope effects are not observed on the he rate constant associated with Co-C bond homolysis as this step is likely gated by the formation of the external aldimine. Stopped-flow kinetics, and Michaelis-Menten steady-state kinetics
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additional information
additional information
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kinetic isotope effects analysis using isotope-labeled DL-ornithine-3,3,4,4,5,5-d6 revealing a diminished Dkcat/Km of 2.5 relative to a Dkcat of 7.6, suggesting slow release of the substrate from the active site. Kinetic isotope effects are not observed on the he rate constant associated with Co-C bond homolysis as this step is likely gated by the formation of the external aldimine. Stopped-flow kinetics, and Michaelis-Menten steady-state kinetics
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additional information
additional information
steady-state and pre-steady-state kinetics
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additional information
additional information
steady-state kinetics of wild-type enzyme and beta-subunit mutants, enzyme dynamics and C-Co bond homolysis in single-turnover stopped-flow kinetics
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