|
|
5.4.3.5 |
Activity |
5.4.3.5 |
Description |
D-ornithine 4,5-aminomutase |
Notes |
A small family built around the validated sequence from clostridium. This is a multi-domain protein. The N-terminal domain is similar to the alfa subunit of D-lysine 5,6-aminomutase (which has a TIM-like barrel fold). The C-terminal domain is similar to the beta subunit of D-lysine 5,6-aminomutase (which has a Rossmann fold). |
PLP Fold Type |
VI |
PLP-dependent Domain |
|
Number of sequences |
5 |
Sequences in seed alignment |
|
Reference sequence |
AAK72502 |
Domain interval |
76-365 |
Catalytic site |
724 K |
| |
References |
Chen HP, Hsui FC, Lin LY, Ren CT, Wu SH. (2004) Coexpression, purification and characterization of the E and S subunits of coenzyme B(12) and B(6) dependent Clostridium sticklandii D-ornithine aminomutase in Escherichia coli Eur J Biochem 271 4293-7. Chen, H. P.; Wu, S. H.; Lin, Y. L.; Chen, C. M.; Tsay, S. S. (2001) Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-ornithine aminomutase from Clostridium sticklandii J Biol Chem 276 44744-50. Articles on 5.4.3.5 |
last changed |
2008/05/13 18:27 |
|