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
-
1,2-amino
-
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
ECTree
5.4.3.5 D-ornithine 4,5-aminomutaseAdvanced search results
results (
results (Engineering
Engineering on EC 5.4.3.5 - D-ornithine 4,5-aminomutase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C700S
site-directed mutagenesis, the beta-subunit mutant shows similar kinetics and activity as the wild-type enzyme
D627A
site-directed mutagenesis, the beta-subunit mutant shows similar kinetics and slightly reduced activity compared to the wild-type enzyme
E338A
E338D
E338Q
E81A
site-directed mutagenesis, inactive beta-subunit mutant
E81D
site-directed mutagenesis, almost inactive beta-subunit mutant
E81Q
site-directed mutagenesis, the beta-subunit mutant shows highly reduced activity compared to wild-type
G128D
site-directed mutagenesis, inactive beta-subunit mutant
G339W
site-directed mutagenesis, the beta-subunit mutant shows altered kinetics and highly reduced activity compared to the wild-type enzyme
I424E
site-directed mutagenesis, the beta-subunit mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N226D
site-directed mutagenesis, the beta-subunit mutant shows highly reduced activity compared to wild-type
P343W
site-directed mutagenesis, the beta-subunit mutant shows altered kinetics and highly reduced activity compared to the wild-type enzyme
R297K
site-directed mutagenesis, almost inactive beta-subunit mutant
S162A
site-directed mutagenesis, the beta-subunit mutant shows highly reduced activity compared to wild-type
Y160F
site-directed mutagenesis, almost inactive beta-subunit mutant
Y187A
site-directed mutagenesis, the beta-subunit mutant shows 1260fold reduced activity, compared to wild-type, attributed to a slower rate of external aldimine formation and a diminution of adenosylcobalamin Co-C bond homolysis
Y187F
E338A
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site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 670fold and catalytic efficiency 220fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
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E338D
E338Q
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site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 90fold and catalytic efficiency 20fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
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E81A
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site-directed mutagenesis, inactive beta-subunit mutant
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E81D
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site-directed mutagenesis, almost inactive beta-subunit mutant
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E81Q
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site-directed mutagenesis, the beta-subunit mutant shows highly reduced activity compared to wild-type
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S162A
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site-directed mutagenesis, the beta-subunit mutant shows highly reduced activity compared to wild-type
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Y160F
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site-directed mutagenesis, almost inactive beta-subunit mutant
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additional information
E338A
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 670fold and catalytic efficiency 220fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
E338A
site-directed mutagenesis, the beta-subunit mutant shows a reduced turnover number compared to wild-type enzyme, while the Km value is similar
E338A
site-directed mutagenesis, the beta-subunit mutant shows altered kinetics and highly reduced activity compared to the wild-type enzyme
E338D
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 380fold and catalytic efficiency 60fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows n detectable adenosylcobalamin homolysis upon binding of the physiological substrate
E338D
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 380fold and catalytic efficiency 60fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
E338D
site-directed mutagenesis, the beta-subunit mutant shows a reduced turnover number compared to wild-type enzyme, while the Km value is similar
E338Q
site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 90fold and catalytic efficiency 20fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
E338Q
site-directed mutagenesis, the beta-subunit mutant shows a reduced turnover number compared to wild-type enzyme, while the Km value is similar
Y187F
site-directed mutagenesis, the beta-subunit mutant shows 25fold reduced activity, compared to wild-type, attributed to a slower rate of external aldimine formation and a diminution of adenosylcobalamin Co-C bond homolysis. In the case of beta-subunit mutant Y187F, the integrity of the active site is maintained as cob(II)alamin and the pyridoxal 5'-phosphate organic radical (even at lower concentrations) remain tightly exchange-coupled
Y187F
site-directed mutagenesis, the beta-subunit mutant shows highly reduced activity compared to wild-type
E338D
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site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 380fold and catalytic efficiency 60fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows n detectable adenosylcobalamin homolysis upon binding of the physiological substrate
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E338D
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site-directed mutagenesis, substrate binding of the mutant is unaffected, but kcat is reduced 380fold and catalytic efficiency 60fold compared to the wild-type enzyme. The rate of external aldimine formation in the mutant is similar to that of the wild-type enzyme, but it shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
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additional information
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protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12800 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation. OraS protein alone lowers the Km of KamDE for adenosylcobalamin and pyridoxal phosphate
additional information
analysis of substrate-bound wild-type and beta-subunit mutant enzymes, overview
additional information
OAM variants are designed to perturb the interface between the cobalamin-binding domain and the pyridoxal 5'-phosphate-binding TIM-barrel domain. Steady-state and single turnover kinetic studies of these variants, combined with pulsed electron-electron double resonance measurements of spin-labeled OAM are used to provide direct evidence for a dynamic interface between the cobalamin and pyridoxal 5'-phosphate-binding domains, overview
