Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.8
Description:Trimethyllysine dioxygenase.
Alternative Name: Trimethyllysine,2-oxoglutarate dioxygenase.
Trimethyllysine alpha-ketoglutarate dioxygenase.
TMLD.
TML-alpha-ketoglutarate dioxygenase.
TML hydroxylase.
TML dioxygenase.
Epsilon-trimethyllysine 2-oxoglutarate dioxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.8
BRENDA Enzyme Link: BRENDA 1.14.11.8
KEGG Enzyme Link: KEGG1.14.11.8
BioCyc Enzyme Link: BioCyc 1.14.11.8
ExPASy Enzyme Link: ExPASy1.14.11.8
EC2PDB Enzyme Link: EC2PDB 1.14.11.8
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.8
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.8
IntEnz Enzyme Link: IntEnz 1.14.11.8
MEDLINE Enzyme Link: MEDLINE 1.14.11.8
MSA:

1.14.11.8;

Phylogenetic Tree:

1.14.11.8;

Uniprot:
M-CSA:
RHEA:14181 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase.Hulse JD, Ellis SR, Henderson LM1978 Mar 10627563
Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis.Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ2001 Sep 711431483
Evidence That Trimethyllysine Hydroxylase Catalyzes the Formation of (2S,3S)-3-Hydroxy-N<sup>ε</sup>-trimethyllysine.Reddy YV, Al Temimi AH, White PB, Mecinović J2017 Jan 2028045275
Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-N<sup>ε</sup>-trimethyllysine.Leśniak RK, Markolovic S, Tars K, Schofield CJ2016 Dec 2227965989
Substrate scope for trimethyllysine hydroxylase catalysis.Al Temimi AH, Pieters BJ, Reddy YV, White PB, Mecinović J2016 Oct 2527730239