دورية أكاديمية
أعرض في EDS

Iron-sulfur cluster engineering provides insight into the evolution of substrate specificity among sulfonucleotide reductases.

التفاصيل البيبلوغرافية
العنوان: Iron-sulfur cluster engineering provides insight into the evolution of substrate specificity among sulfonucleotide reductases.
المؤلفون: Bhave DP; Chemical Biology Graduate Program, University of Michigan, Ann Arbor, Michigan 48109, United States., Hong JA, Keller RL, Krebs C, Carroll KS
المصدر: ACS chemical biology [ACS Chem Biol] 2012 Feb 17; Vol. 7 (2), pp. 306-15. Date of Electronic Publication: 2011 Nov 09.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c2006-
مواضيع طبية MeSH: Bacteria/*enzymology , Bacterial Proteins/*chemistry , Iron-Sulfur Proteins/*chemistry , Oxidoreductases/*chemistry , Oxidoreductases Acting on Sulfur Group Donors/*chemistry, Amino Acid Motifs ; Bacterial Proteins/metabolism ; Iron-Sulfur Proteins/metabolism ; Models, Molecular ; Oxidoreductases/metabolism ; Oxidoreductases Acting on Sulfur Group Donors/metabolism ; Protein Structure, Tertiary ; Substrate Specificity
مستخلص: Assimilatory sulfate reduction supplies prototrophic organisms with reduced sulfur that is required for the biosynthesis of all sulfur-containing metabolites, including cysteine and methionine. The reduction of sulfate requires its activation via an ATP-dependent activation to form adenosine-5'-phosphosulfate (APS). Depending on the species, APS can be reduced directly to sulfite by APS reductase (APR) or undergo a second phosphorylation to yield 3'-phosphoadenosine-5'-phosphosulfate (PAPS), the substrate for PAPS reductase (PAPR). These essential enzymes have no human homologue, rendering them attractive targets for the development of novel antibacterial drugs. APR and PAPR share sequence and structure homology as well as a common catalytic mechanism, but the enzymes are distinguished by two features, namely, the amino acid sequence of the phosphate-binding loop (P-loop) and an iron-sulfur cofactor in APRs. On the basis of the crystal structures of APR and PAPR, two P-loop residues are proposed to determine substrate specificity; however, this hypothesis has not been tested. In contrast to this prevailing view, we report here that the P-loop motif has a modest effect on substrate discrimination. Instead, by means of metalloprotein engineering, spectroscopic, and kinetic analyses, we demonstrate that the iron-sulfur cluster cofactor enhances APS reduction by nearly 1000-fold, thereby playing a pivotal role in substrate specificity and catalysis. These findings offer new insights into the evolution of this enzyme family and extend the known functions of protein-bound iron-sulfur clusters.
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معلومات مُعتمدة: R01 GM087638 United States GM NIGMS NIH HHS; R01 GM087638-03S1 United States GM NIGMS NIH HHS; R01 GM087638-04 United States GM NIGMS NIH HHS; GM087638 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Iron-Sulfur Proteins)
EC 1.- (Oxidoreductases)
EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors)
EC 1.8.4.- (3'-phosphoadenylyl-5'-phosphosulfate reductase)
EC 1.8.99.2 (adenylylsulfate reductase)
تواريخ الأحداث: Date Created: 20111026 Date Completed: 20120605 Latest Revision: 20240412
رمز التحديث: 20240412
مُعرف محوري في PubMed: PMC3288176
DOI: 10.1021/cb200261n
PMID: 22023093
قاعدة البيانات: MEDLINE
الوصف
تدمد:1554-8937
DOI:10.1021/cb200261n