Synonyms: D-ornithine 4,5-aminomutase
Species: [Clostridium] sticklandii
Subunit composition of
D-ornithine aminomutase = [OraE]2[OraS]2
D-ornithine aminomutase component E subunit = OraE (summary available)
D-ornithine aminomutase component S subunit = OraS
D-Ornithine 4,5-aminomutase catalyzes the conversion of D-ornithine to D-threo-2,4-diaminopentanoate as part of the pathway of ornithine oxidation. The enzyme contains pyridoxal phosphate and tightly bound cobamide. It is specific for D-ornithine [Somack73, Kenklies99, Dyer68, Dyer70, Jeng74].
This enzyme was previously reported to be a homodimer [Somack73], but is now believed to be an α2β2 heterotetramer [Chen01]. The molecular weight of the complex was estimated by gel filtration chromatography (in [Chen01]).
Molecular Weight: 200 kD (experimental) [Chen01 ]
Enzymatic reaction of: D-ornithine aminomutase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
This reaction is reversible.
Inhibitors (Unknown Mechanism): L-α-ornithine [Somack73] , L-α-lysine [Somack73] , D,L-α-lysine [Somack73] , β-L-lysine [Somack73] , oxygen [Somack73] , isoniazid [Somack73] , hydroxylamine [Somack73] , p-chloromercuribenzoate [Somack73] , N-ethylmaleimide [Somack73] , iodoacetate
Primary Physiological Regulators of Enzyme Activity: L-α-ornithine, L-α-lysine, D,L-α-lysine, β-L-lysine, oxygen
|Gene:||oraE||Accession Number: G-9593 (MetaCyc)|
Molecular Weight: 83.05 kD (from nucleotide sequence)
Relationship Links: InterPro:IN-FAMILY:IPR006158 , InterPro:IN-FAMILY:IPR015130 , InterPro:IN-FAMILY:IPR016176 , PDB:Structure:3KOW , PDB:Structure:3KOX , PDB:Structure:3KOY , PDB:Structure:3KOZ , PDB:Structure:3KP0 , PDB:Structure:3KP1 , Pfam:IN-FAMILY:PF02310 , Pfam:IN-FAMILY:PF09043 , Prosite:IN-FAMILY:PS51332
This subunit contains a conserved, base-off/histidine-on cobalamin-binding motif, GXDXHXXG, at the C-terminus [Chen01].
|Gene:||oraS||Accession Number: G-9592 (MetaCyc)|
Molecular Weight: 13.623 kD (from nucleotide sequence)
Unification Links: UniProt:Q8VPJ6
Chen01: Chen HP, Wu SH, Lin YL, Chen CM, Tsay SS (2001). "Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-ornithine aminomutase from Clostridium sticklandii." J Biol Chem 276(48);44744-50. PMID: 11577113
Jeng74: Jeng IM, Somack R, Barker HA (1974). "Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl coenzyme A." Biochemistry 1974;13(14);2898-903. PMID: 4407783
Kenklies99: Kenklies J, Ziehn R, Fritsche K, Pich A, Andreesen JR (1999). "Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC." Microbiology 1999;145 ( Pt 4);819-26. PMID: 10220161
Somack73: Somack R, Costilow RN (1973). "Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5,4-aminomutase." Biochemistry 1973;12(14);2597-604. PMID: 4711468
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493