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
-
homolysis
- 5'-phosphate
-
plp-dependent
-
5,6-aminomutase
-
aldimine
-
rossmann
-
radical-based
-
stopped-flow
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5\'-deoxyadenosyl
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paramagnetic
-
1,2-amino
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deprotonated
- d-lysine
-
cobalamin-binding
-
rupture
- ribose
- imine
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interconverting
-
5\'-deoxyadenosylcobalamin
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multistep
-
adocbl-dependent
-
isomerization
- pyridoxal-5'-phosphate
- pyridine
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uv-visible
-
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 (Substrates Products
Substrates Products on EC 5.4.3.5 - D-ornithine 4,5-aminomutase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DL-ornithine
(2R,4S)-2,4-diaminopentanoate
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-
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r
D-ornithine
(2R,4S)-2,4-diaminopentanoate
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-
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r
D-ornithine
(2R,4S)-2,4-diaminopentanoate
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-
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r
D-ornithine
(2R,4S)-2,4-diaminopentanoate
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second step in the oxidation pathway of L-ornithine
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r
D-ornithine
(2R,4S)-2,4-diaminopentanoate
binding of substrate to the enzyme leads to the formation of an electrostatic interaction between a conserved glutamate side chain and the adenosyl ribose of the adenosylcobalamin cofactor. Residue Glu338 is involved in adenosylcobalamin Co-C bond labilization and catalysis
-
-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
the 1,2-amino shift performed by the enzyme is considered energetically challenging as it involves breakage of chemically inert C-H and C-N bonds. OAM overcomes this thermodynamic barrier with radical-based catalysis that is initiated and propagated by the enzyme's adenosylcobalamin and pyridoxal 5'-phosphate cofactors, conformational change upon substrate binding, overview
-
-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
the 1,2-amino shift performed by the enzyme is considered energetically challenging as it involves breakage of chemically inert CH and CN bonds. OAM overcomes this thermodynamic barrier with radical-based catalysis that is initiated and propagated by the enzyme's adenosylcobalamin and pyridoxal 5'-phosphate cofactors, conformational change upon substrate binding, overview
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-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
-
the enzyme is highly specific for D-ornithine as a substrate, substrate binding structure, overview
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-
r
D-ornithine
(2R,4S)-2,4-diaminopentanoate
-
-
-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
binding of substrate to the enzyme leads to the formation of an electrostatic interaction between a conserved glutamate side chain and the adenosyl ribose of the adenosylcobalamin cofactor. Residue Glu338 is involved in adenosylcobalamin Co-C bond labilization and catalysis
-
-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
-
-
-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
the 1,2-amino shift performed by the enzyme is considered energetically challenging as it involves breakage of chemically inert CH and CN bonds. OAM overcomes this thermodynamic barrier with radical-based catalysis that is initiated and propagated by the enzyme's adenosylcobalamin and pyridoxal 5'-phosphate cofactors, conformational change upon substrate binding, overview
-
-
?
D-ornithine
(2R,4S)-2,4-diaminopentanoate
-
-
-
r
D-ornithine
(2R,4S)-2,4-diaminopentanoate
the 1,2-amino shift performed by the enzyme is considered energetically challenging as it involves breakage of chemically inert C-H and C-N bonds. OAM overcomes this thermodynamic barrier with radical-based catalysis that is initiated and propagated by the enzyme's adenosylcobalamin and pyridoxal 5'-phosphate cofactors, conformational change upon substrate binding, overview
-
-
?
additional information
?
-
-
subunit OraS of the enzyme is capable of forming a complex with recombinant enzyme (KamDE) containing only E1 of lysine 5,6-aminomutase, EC 5.4.3.4, and restores its allosteric regulation by ATP
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-
?
additional information
?
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adenosylcobalamin-dependent ornithine 4,5-aminomutase from Clostridium sticklandii utilizes pyridoxal 5'-phosphate to interconvert D-ornithine to 2,4-diaminopentanoate via a multistep mechanism that involves two hydrogen transfer steps. Important role of enzyme residue tyrosine 187, which lies planar to the pyridoxal 5'-phosphate pyridine ring. Coupled enzyme assay of ornithine 4,5-aminomutase with 2,4-diaminopentanoate dehydrogenase with DL-ornithine and DL-ornithine-3,3,4,4,5,5-d6 as substrates
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-
?
additional information
?
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-
adenosylcobalamin-dependent ornithine 4,5-aminomutase from Clostridium sticklandii utilizes pyridoxal 5'-phosphate to interconvert D-ornithine to 2,4-diaminopentanoate via a multistep mechanism that involves two hydrogen transfer steps. Important role of enzyme residue tyrosine 187, which lies planar to the pyridoxal 5'-phosphate pyridine ring. Coupled enzyme assay of ornithine 4,5-aminomutase with 2,4-diaminopentanoate dehydrogenase with DL-ornithine and DL-ornithine-3,3,4,4,5,5-d6 as substrates
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-
?
additional information
?
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cobalamin-dependent enzymes enhance the rate of C-Co bond cleavage by up to 1012-fold to generate cob(II)alamin and a transient adenosyl radical. In the case of the pyridoxal 5'-phosphate and cobalamin-dependent enzymes lysine 5,6-aminomutase (EC 5.4.3.3) and ornithine 4,5 aminomutase, it has been proposed that a large scale domain reorientation of the cobalamin-binding domain is linked to radical catalysis Coupled enzyme assay with (2R,4S)-2,4-diaminopentanoate dehydrogenase (DAPDH) from Clostridium difficile
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?
additional information
?
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enzyme OAM is highly specific for D-ornithine, which forms non-covalent interactions with R297 and E81 through its alpha-amine and alpha-carboxylate groups. Neither wild type enzyme OAM nor any of the R297 or E81 variants are active towards the larger substrate
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-
?
additional information
?
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enzyme OAM is highly specific for D-ornithine, which forms non-covalent interactions with R297 and E81 through its alpha-amine and alpha-carboxylate groups. Neither wild type enzyme OAM nor any of the R297 or E81 variants are active towards the larger substrate
-
-
?
additional information
?
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enzyme OAM is highly specific for D-ornithine, which forms non-covalent interactions with R297 and E81 through its alpha-amine and alpha-carboxylate groups. Neither wild type enzyme OAM nor any of the R297 or E81 variants are active towards the larger substrate
-
-
?
