H
IPR038492

GBBH-like, N-terminal domain superfamily

InterPro entry
Short nameGBBH-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

3.A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases. Rajakovich LJ, Pandelia ME, Mitchell AJ, Chang WC, Zhang B, Boal AK, Krebs C, Bollinger JM Jr. Biochemistry 58, 1627-1647, (2019). PMID: 30789718

Cross References

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