|Gene:||dapL||Accession Numbers: G-12008 (MetaCyc), MJ1391|
Species: Methanocaldococcus jannaschii
Organisms that synthesize L-lysine via the lysine biosynthesis VI pathway use the enzyme L,L-diaminopimelate aminotransferase to catalyze the direct conversion of (S)-2,3,4,5-tetrahydrodipicolinate to L,L-diaminopimelate. The pathway, which was originally characterized in green plants, is also used by certain bacteria, and some archaeabacteria belonging to the Methanobacteria and Methanococci classes.
The dapL gene from Methanocaldococcus jannaschii was cloned, expressed in Escherichia coli and purified. The protein was stable at 100° C for at least 30 min, and maximal activity was observed at 70° C. The enzyme was not able to use succinyl-DAP or acetyl-DAP as a substrate [Liu10a].
Molecular Weight of Polypeptide: 47.709 kD (from nucleotide sequence)
Relationship Links: InterPro:IN-FAMILY:IPR004838 , InterPro:IN-FAMILY:IPR004839 , InterPro:IN-FAMILY:IPR015421 , InterPro:IN-FAMILY:IPR015422 , InterPro:IN-FAMILY:IPR015424 , Pfam:IN-FAMILY:PF00155 , Prosite:IN-FAMILY:PS00105
Enzymatic reaction of: L,L-diaminopimelate aminotransferase
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
This reaction is reversible.
In Pathways: lysine biosynthesis VI
T(opt): 70 °C [Liu10a]
pH(opt): 8-9 [Liu10a]
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493