IPR038492
GBBH-like, N-terminal domain superfamily
InterPro entry
Short name | GBBH-like_N_sf |
Overlapping entries |
Description
Gamma-butyrobetaine hydroxylase (GBBH), also known as gamma-butyrobetaine dioxygenase, is an alpha-ketoglutarate-dependent dioxygenase that catalyses the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded β-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain facilitates the assembly of a symmetric head-to-tail dimer formation through the interface with the C-terminal domain of the other monomer
[1, 3].
This domain superfamily is also found in another hydroxylase of the biosynthetic pathway of L-carnitine, the first enzyme of the pathway, known as trimethyllysine dioxygenase (TMLD). Like GBBH, TMLD is a non-heme ferrous-iron dioxygenase that requires alpha-ketoglutarate, Fe2+, and molecular oxygen as cofactors
[2].
References
1.Crystal structure of human gamma-butyrobetaine hydroxylase. Tars K, Rumnieks J, Zeltins A, Kazaks A, Kotelovica S, Leonciks A, Sharipo J, Viksna A, Kuka J, Liepinsh E, Dambrova M. Biochem. Biophys. Res. Commun. 398, 634-9, (2010). View articlePMID: 20599753
2.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 RJ. J. Biol. Chem. 276, 33512-7, (2001). View articlePMID: 11431483
Cross References
ENZYME
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.30.2020.30