 |
InterPro: IPR016084 Haem oxygenase-like, multi-helical
Protein matches
|
UniProtKB Matches: 2166 proteins |
|
|
Accession
|
IPR016084 Haem_Oase-like_multi-hlx |
|
Type
|
Domain |
|
Signatures
|
|
|
InterPro Relationships
|
|
Children
|
IPR004305 TENA/THI-4 protein/Coenzyme PQQ biosynthesis protein C
|
|
Found in
|
IPR002051 Haem oxygenase
IPR016951 Haem oxygenase (decyclizing), plant
|
|
Contains
|
IPR018207 Haem oxygenase conserved site
|
|
InterPro annotation
|
|
 Entry Details in BioMart
|
|
Abstract
|
This entry represents a multi-helical structural domain consisting of two structural repeats (duplication) of a 3-helical motif. This domain can be found in both eukaryotic and prokaryotic haem oxygenases [1, 2], in TENA/THI-4 proteins that lack the haem-binding site [3], and in coenzyme PQQ (pyrrolo-quinoline-quinone) biosynthesis protein C (PqqC) [4].
Haem oxygenase (EC:1.14.99.3) (HO) is the microsomal enzyme that, in animals, carries out the oxidation of haem, cleaving the haem ring at the alpha-methene bridge to form biliverdin and carbon monoxide. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. In mammals there are three isozymes of haem oxygenase: HO-1 to HO-3. The first two isozymes differ in their tissue expression and their inducibility: HO-1 is highly inducible by its substrate haem and by various non-haem substances, while HO-2 is non-inducible. Haem oxygenase is also present in certain bacteria, where it is involved in the acquisition of iron from the host haem.
The THI-4 protein is involved in thiamine biosynthesis, while TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase.
Coenzyme PQQ (pyrrolo-quinoline-quinone) biosynthesis protein C (PqqC; EC:1.3.3.11) is required for the synthesis of PQQ, where PQQ is a prosthetic group found in several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria.
|
|
Structural links
|
|
|
Publications
|
|
1.
|
Lad L, Friedman J, Li H, Bhaskar B, Ortiz de Montellano PR, Poulos TL.
Crystal structure of human heme oxygenase-1 in a complex with biliverdin.
Biochemistry 43 3793-801 2004
[PubMed: 15049686]
http://dx.doi.org/10.1021/bi035451l
|
|
2.
|
Schuller DJ, Zhu W, Stojiljkovic I, Wilks A, Poulos TL.
Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1.
Biochemistry 40 11552-8 2001
[PubMed: 11560504]
http://dx.doi.org/10.1021/bi0110239
|
|
3.
|
Benach J, Edstrom WC, Lee I, Das K, Cooper B, Xiao R, Liu J, Rost B, Acton TB, Montelione GT, Hunt JF.
The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism.
Acta Crystallogr. D Biol. Crystallogr. 61 589-98 2005
[PubMed: 15858269]
http://dx.doi.org/10.1107/S0907444905005147
|
|
4.
|
Magnusson OT, Toyama H, Saeki M, Rojas A, Reed JC, Liddington RC, Klinman JP, Schwarzenbacher R.
Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone.
Proc. Natl. Acad. Sci. U.S.A. 101 7913-8 2004
[PubMed: 15148379]
http://dx.doi.org/10.1073/pnas.0402640101
|
|
Additional Reading
|
|
Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr.
Ensemble refinement of protein crystal structures: validation and application.
Structure 15 2007 1040-52
[PubMed: 17850744]
http://dx.doi.org/10.1016/j.str.2007.06.019
|
|
|
Sugishima M, Higashimoto Y, Oishi T, Takahashi H, Sakamoto H, Noguchi M, Fukuyama K.
X-ray crystallographic and biochemical characterization of the inhibitory action of an imidazole-dioxolane compound on heme oxygenase.
Biochemistry 46 2007 1860-7
[PubMed: 17253780]
http://dx.doi.org/10.1021/bi062264p
|
|
|
Sugishima M, Oda K, Ogura T, Sakamoto H, Noguchi M, Fukuyama K.
Alternative cyanide-binding modes to the haem iron in haem oxygenase.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 471-4
[PubMed: 17554165]
|
|
|
Jenkins AL, Zhang Y, Ealick SE, Begley TP.
Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.
Bioorg. Chem. 36 2008 29-32
[PubMed: 18054064]
http://dx.doi.org/10.1016/j.bioorg.2007.10.005
|
|
|
Rahman MN, Vlahakis JZ, Szarek WA, Nakatsu K, Jia Z.
X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors.
J. Med. Chem. 51 2008 5943-52
[PubMed: 18798608]
http://dx.doi.org/10.1021/jm800505m
|
|
|
InterPro 23.1
|
