NDLI: Starter unit specificity directs genome mining of polyketide synthase pathways in fungi.

Please wait, while we are loading the content...

Starter unit specificity directs genome mining of polyketide synthase pathways in fungi.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Crawford, Jason M. Vagstad, Anna L. Ehrlich, Kenneth C. Townsend, Craig A.
Description	Country affiliation: United States Author Affiliation: Crawford JM ( Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.)
Abstract	Search of the protein database with the aflatoxin pathway polyketide synthase (PKS) revealed putative PKSs in the pathogenic fungi Coccidioides immitis and Coccidioides posadasii that could require partnerships with a pair of fatty acid synthase (FAS) subunits for the biosynthesis of fatty acid-polyketide hybrid metabolites. A starter unit:acyl-carrier protein transacylase (SAT) domain was discovered in the nonreducing PKS. This domain is thought to accept the fatty acid product from the FAS to initiate polyketide synthesis. We expressed the C. immitis SAT domain in Escherichia coli and showed that this domain, unlike that from the aflatoxin pathway PKS, transferred octanoyl-CoA four times faster than hexanoyl-CoA. The SAT domain also formed a covalent octanoyl intermediate and transferred this group to a free-standing ACP domain. Our results suggest that C. immitis/posadasii, both human fungal pathogens, contain a FAS/PKS cluster with functional similarity to the aflatoxin cluster found in Aspergillus species. Dissection of the PKS and determination of in vitro SAT domain specificity provides a tool to uncover the growing number of similar sequenced pathways in fungi, and to guide elucidation of the fatty acid-polyketide hybrid metabolites that they produce.
File Format	HTM / HTML
ISSN	00452068
e-ISSN	10902120
DOI	10.1016/j.bioorg.2007.11.002
Journal	Bioorganic Chemistry
Issue Number	1
Volume Number	36
Language	English
Publisher	Elsevier
Publisher Date	2008-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Coccidioides Genetics Metabolism Genome, Fungal Polyketide Synthases Signal Transduction Acyl Coenzyme A Acyltransferases Aflatoxins Binding Sites Classification Databases, Protein Escherichia Coli Enzymology Fatty Acid Synthases Fatty Acids Protein Structure, Tertiary Substrate Specificity Research Support, N.i.h., Extramural Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Drug Discovery Molecular Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Starter unit specificity directs genome mining of polyketide synthase pathways in fungi

An acyltransferase domain of FK506 polyketide synthase recognizing both an acyl carrier protein and coenzyme A as acyl donors to transfer allylmalonyl and ethylmalonyl units

Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase.

Probing the interactions of an acyl carrier protein domain from the 6-deoxyerythronolide B synthase.

Fatty acyl-AMP ligases and polyketide synthases are unique enzymes of lipid biosynthetic machinery in Mycobacterium tuberculosis.

Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.

Protein-Protein Recognition between Acyltransferases and Acyl Carrier Proteins in Multimodular Polyketide Synthases †

ASMPKS: an analysis system for modular polyketide synthases

Biochemistry. Anatomy of a fungal polyketide synthase.

Starter unit specificity directs genome mining of polyketide synthase pathways in fungi.

Similar Documents

Starter unit specificity directs genome mining of polyketide synthase pathways in fungi

An acyltransferase domain of FK506 polyketide synthase recognizing both an acyl carrier protein and coenzyme A as acyl donors to transfer allylmalonyl and ethylmalonyl units

Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase.

Probing the interactions of an acyl carrier protein domain from the 6-deoxyerythronolide B synthase.

Fatty acyl-AMP ligases and polyketide synthases are unique enzymes of lipid biosynthetic machinery in Mycobacterium tuberculosis.

Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.

Protein-Protein Recognition between Acyltransferases and Acyl Carrier Proteins in Multimodular Polyketide Synthases †

ASMPKS: an analysis system for modular polyketide synthases

Biochemistry. Anatomy of a fungal polyketide synthase.

Starter unit specificity directs genome mining of polyketide synthase pathways in fungi.