(+)-exo-5-hydroxycamphor

(+)-exo-5-hydroxycamphor is a lipid of Prenol Lipids (PR) class. The associated genes with (+)-exo-5-hydroxycamphor are putidaredoxin.

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Introduction

To understand associated biological information of (+)-exo-5-hydroxycamphor, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with (+)-exo-5-hydroxycamphor?

There are no associated biomedical information in the current reference collection.

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with (+)-exo-5-hydroxycamphor

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with (+)-exo-5-hydroxycamphor?

There are no associated biomedical information in the current reference collection.

What functions are associated with (+)-exo-5-hydroxycamphor?

There are no associated biomedical information in the current reference collection.

What lipids are associated with (+)-exo-5-hydroxycamphor?

There are no associated biomedical information in the current reference collection.

What genes are associated with (+)-exo-5-hydroxycamphor?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with (+)-exo-5-hydroxycamphor?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with (+)-exo-5-hydroxycamphor

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Authors Title Published Journal PubMed Link
Yang W et al. The structure of CYP101D2 unveils a potential path for substrate entry into the active site. 2011 Biochem. J. pmid:20950270
Bell SG et al. A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans. 2010 Appl. Microbiol. Biotechnol. pmid:19779713
Kim D and Ortiz de Montellano PR Tricistronic overexpression of cytochrome P450cam, putidaredoxin, and putidaredoxin reductase provides a useful cell-based catalytic system. 2009 Biotechnol. Lett. pmid:19458919
Persson B et al. Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily. 2008 Cell. Mol. Life Sci. pmid:19011751
Zhang W et al. Solution NMR structure of putidaredoxin-cytochrome P450cam complex via a combined residual dipolar coupling-spin labeling approach suggests a role for Trp106 of putidaredoxin in complex formation. 2008 J. Mol. Biol. pmid:18835276
Nodate M et al. Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784. 2006 Appl. Microbiol. Biotechnol. pmid:16195793
Rui L et al. Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity. 2006 Biochemistry pmid:16548516
Kamachi T and Yoshizawa K A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome p450. 2003 J. Am. Chem. Soc. pmid:12683838
Davydov R et al. Hydroxylation of camphor by reduced oxy-cytochrome P450cam: mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes. 2001 J. Am. Chem. Soc. pmid:11456714
Bell SG et al. Engineering the CYP101 system for in vivo oxidation of unnatural substrates. 2001 Protein Eng. pmid:11739899