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Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulatin...

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulatin...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b469b0462bc94b0e8a1d29a9113fb32b

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

About this item

Full title

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2020-06, Vol.11 (1), p.2813-12, Article 2813

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

5′-aminolevulinate synthase (ALAS) catalyzes the first step in heme biosynthesis, generating 5′-aminolevulinate from glycine and succinyl-CoA. Inherited frameshift indel mutations of human erythroid-specific isozyme ALAS2, within a C-terminal (Ct) extension of its catalytic core that is only present in higher eukaryotes, lead to gain-of-function X-...

Alternative Titles

Full title

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_b469b0462bc94b0e8a1d29a9113fb32b

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b469b0462bc94b0e8a1d29a9113fb32b

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-020-16586-x

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