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5.4.3.5 D-ornithine 4,5-aminomutase.
Bioparts catalyze this reaction
Biopart ID | Organisms | pH | temperature(ºC) | km |
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Qualitative and quantitative parameters:
Temperature
-
37.0
pH
-
9.0
Taxonomy
Protein sequence
Sequence
Protein family
Protein structure
Nucleotide sequences (Optimized nucleotide sequences according to different chassises)
Sequence
- R Somack; R N Costilow; . 1973: Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5,4-aminomutase. Biochemistry, 12 2597-604.
- H P Chen; S H Wu; Y L Lin; C M Chen; S S Tsay; . 2001: Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-ornithine aminomutase from Clostridium sticklandii. The Journal of Biological Chemistry, 276 44744-50.
- Kirsten R Wolthers; Colin Levy; Nigel S Scrutton; David Leys; . 2010: Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase. The Journal of Biological Chemistry, 285 13942-50.
- Nuria Fonknechten; Sébastien Chaussonnerie; Sabine Tricot; Aurélie Lajus; Jan R Andreesen; Nadia Perchat; Eric Pelletier; Michel Gouyvenoux; Valérie Barbe; Marcel Salanoubat; Denis Le Paslier; Jean Weissenbach; Georges N Cohen; Annett Kreimeyer; . 2010: Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence. BMC Genomics, 11 555.