Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

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, Jeng74a].

This enzyme was previously reported to be a homodimer [Somack73], but is now believed to be an α2β2 heterotetramer [Chen01a]. The molecular weight of the complex was estimated by gel filtration chromatography (in [Chen01a]).

Molecular Weight: 200 kD (experimental) [Chen01a ]

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
[Chen01a]


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 [Chen01a].


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

Chen01a: 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

Jeng74a: 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 Fri Nov 28, 2014, biocyc13.