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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: D-ornithine aminomutase

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

Summary:
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 [Chen01c]. The molecular weight of the complex was estimated by gel filtration chromatography (in [Chen01c]).

Molecular Weight: 200 kD (experimental) [Chen01c ]

Gene-Reaction Schematic: ?

Credits:
Last-Curated ? 21-Sep-2006 by Fulcher CA , SRI International


Enzymatic reaction of: D-ornithine aminomutase

EC Number: 5.4.3.5

D-ornithine <=> (2R,4S)-2, 4-diaminopentanoate

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.

In Pathways: arginine, ornithine and proline interconversion , ornithine degradation II (Stickland reaction)

Cofactors or Prosthetic Groups: coenzyme B12 [Somack73], pyridoxal 5'-phosphate [Somack73]

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

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-ornithine
44.5
[Chen01c]


Subunit of D-ornithine aminomutase: D-ornithine aminomutase component E subunit

Synonyms: OraE

Gene: oraE Accession Number: G-9593 (MetaCyc)

Molecular Weight: 83.05 kD (from nucleotide sequence)

Unification Links: Protein Model Portal:E3PY95 , UniProt:Q8VPJ5

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

Summary:
This subunit contains a conserved, base-off/histidine-on cobalamin-binding motif, GXDXHXXG, at the C-terminus [Chen01c].


Subunit of D-ornithine aminomutase: D-ornithine aminomutase component S subunit

Synonyms: OraS

Gene: oraS Accession Number: G-9592 (MetaCyc)

Molecular Weight: 13.623 kD (from nucleotide sequence)

Unification Links: UniProt:Q8VPJ6

Relationship Links: InterPro:IN-FAMILY:IPR016176 , PDB:Structure:3KOW , PDB:Structure:3KOX , PDB:Structure:3KOY , PDB:Structure:3KOZ , PDB:Structure:3KP0 , PDB:Structure:3KP1


References

Chen01c: 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

Dyer68: Dyer JK, Costilow RN (1968). "Fermentation of ornithine by Clostridium sticklandii." J Bacteriol 1968;96(5);1617-22. PMID: 5726303

Dyer70: Dyer JK, Costilow RN (1970). "2,4-diaminovaleric acid: an intermediate in the anaerobic oxidation of ornithine by Clostridium sticklandii." J Bacteriol 1970;101(1);77-83. PMID: 4312545

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC14B.