11 β- hydroxysteroid dehydrogenase 1

11 β- hydroxysteroid dehydrogenase 1
other names	11 β -HSD1
	Existing structural data: s. UniProt
Properties of human protein
Mass / length primary structure	291 amino acids
Secondary to quaternary structure	Homodimer; single-pass membrane protein (ER)
Identifier
Gene name	HSD11B1
External IDs	OMIM : 600713 ; UniProt : P28845 ;
Enzyme classification
EC, category	1.1.1.146 , oxidoreductase
Response type	Dehydration
Substrate	11beta-hydroxysteroid + NAD +
Products	11-oxosteroid + NADPH / H +
Occurrence
Parent taxon	Eukaryotes
	Orthologue

The 11 β -hydroxysteroid dehydrogenase 1 (in short: 11 β -HSD1 ) is the isoform 1 of the 11 β -HSD and is among the eukaryotes - enzymes . The enzyme catalyzes the conversion of cortisol to cortisone and plays a role in the regulation of cortisone activity. It is a membrane protein of the endoplasmic reticulum . Mutations in the HSD11B1 gene are responsible for the so-called AME syndrome , a form of hyperandrogenism and a rare hereditary disease.

Occurrence

11 β -HSD1 is greatly in humans in the liver , the adipose tissue and the central nervous system expressed . It is also produced in human skin .

Inhibitors

One of the known inhibitors of the 11 β -HSD1 is 18 α - glycyrrhetinic acid . A study from 2014 found that the epigallocatechin gallate of green tea , the enzymatic activity of 11 β inhibits HSD1. This could explain some of the health benefits of green tea.

Catalyzed reactions of the 11 β- HSD isoforms

The conversion of cortisol into cortisone is of the NAD ⁺ -dependent 11 β -HSD2 catalyzed. The conversion of cortisone to cortisol, however, catalyses the NADPH -dependent 11 β -HSD1:

+ NAD ⁺ + NADPH / H ⁺ ${\ displaystyle \ leftrightharpoons}$

Individual evidence

↑ Homologues at inParanoid
↑ UniProt P28845
^ ^A ^b Jan Behrends, Josef Bischofberger, Rainer Deutzmann, Heimo Ehmke, Stephan Frings: 11. Hormonelle Regulation In: Duale Reihe Physiologie , 2nd edition, Georg Thieme Verlag 2012; P. 380. ISBN 9783131384126 .
↑ Classen-Houben D., Schuster D., Da Cunha T. et al. : Selective inhibition of 11beta-hydroxysteroid dehydrogenase 1 by 18alpha-glycyrrhetinic acid but not 18beta-glycyrrhetinic acid. . In: J Steroid Biochem Mol Biol . 113, No. 3-5, February 2009, pp. 248-252. doi : 10.1016 / j.jsbmb.2009.01.009 . PMID 19429429 .
↑ Jan Hintzpeter, Claudia Stapelfeld, Christine Loerz, Hans-Joerg Martin, Edmund Maser: Green Tea and One of Its Constituents, Epigallocatechine-3-gallate, Are Potent Inhibitors of Human 11β-hydroxysteroid Dehydrogenase Type 1. In: PLoS ONE. 9, 2014, p. E84468, doi : 10.1371 / journal.pone.0084468 .

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Steroid Hormone Metabolism - Learning and Teaching Materials

Jassal / reactome: Oxidation of cortisol to yield cortisone

[1] Homologues at inParanoid

[2] UniProt P28845

[Duale_Reihe_Physiologie-3] A ^b Jan Behrends, Josef Bischofberger, Rainer Deutzmann, Heimo Ehmke, Stephan Frings: 11. Hormonelle Regulation In: Duale Reihe Physiologie , 2nd edition, Georg Thieme Verlag 2012; P. 380. ISBN 9783131384126 .

[4] Classen-Houben D., Schuster D., Da Cunha T. et al. : Selective inhibition of 11beta-hydroxysteroid dehydrogenase 1 by 18alpha-glycyrrhetinic acid but not 18beta-glycyrrhetinic acid. . In: J Steroid Biochem Mol Biol . 113, No. 3-5, February 2009, pp. 248-252. doi : 10.1016 / j.jsbmb.2009.01.009 . PMID 19429429 .

[DOI10.1371/journal.pone.0084468-5] Jan Hintzpeter, Claudia Stapelfeld, Christine Loerz, Hans-Joerg Martin, Edmund Maser: Green Tea and One of Its Constituents, Epigallocatechine-3-gallate, Are Potent Inhibitors of Human 11β-hydroxysteroid Dehydrogenase Type 1. In: PLoS ONE. 9, 2014, p. E84468, doi : 10.1371 / journal.pone.0084468 .