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TMLHE  -  trimethyllysine hydroxylase, epsilon

Homo sapiens

Synonyms: AUTSX6, BBOX2, Epsilon-trimethyllysine 2-oxoglutarate dioxygenase, Epsilon-trimethyllysine hydroxylase, FLJ10727, ...
 
 
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High impact information on TMLHE

  • Otherwise from all the other enzymes of carnitine biosynthesis, TMLH was found to be associated to the mitochondrial fraction [1].
  • As great interest, we found that TMLH-b and TMLH-H389L, individually co-expressed with TMLH-a in COS-1 cells, negatively affect TMLH activity [1].
  • We here report molecular cloning of two alternative spliced forms of TMLH, which appear ubiquitously expressed in human adult and fetal tissues [1].
  • epsilon-N-Trimethyllysine hydroxylase (TMLH) (EC 1.14.11.8) is a non-heme-ferrous iron hydroxylase, Fe(++) and 2-oxoglutarate (2OG) dependent, catalyzing the first of four enzymatic reactions of the highly conserved carnitine biosynthetic pathway [1].
  • In vitro experiments in adhesion and ELISA assays revealed that the TMLD-containing disintegrins, VLO5 and EO5, appeared to be very potent inhibitors of human alpha4beta1 and alpha9beta1 and less effective in inhibition of the alpha4beta7 integrin [2].

References

  1. Functional analysis of TMLH variants and definition of domains required for catalytic activity and mitochondrial targeting. Monfregola, J., Cevenini, A., Terracciano, A., van Vlies, N., Arbucci, S., Wanders, R.J., D'Urso, M., Vaz, F.M., Ursini, M.V. J. Cell. Physiol. (2005) [Pubmed]
  2. Structural requirements of MLD-containing disintegrins for functional interaction with alpha 4 beta 1 and alpha 9 beta1 integrins. Bazan-Socha, S., Kisiel, D.G., Young, B., Theakston, R.D., Calvete, J.J., Sheppard, D., Marcinkiewicz, C. Biochemistry (2004) [Pubmed]
 
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