Investigation of an octapeptide inhibitor of Escherichia coli ribonucleotide reductase by transferred nuclear Overhauser effect spectroscopy

Journal Article · Tue Aug 20 04:00:00 EDT 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00247a008· OSTI ID:5822309

Bushweller, J H; Bartlett, P A ^[1]

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1. Univ. of California, Berkeley (United States)

Several peptides contained within the C-terminal sequence of the B2 subunit of Escherichia coli ribonucleotide reductase (RNR) were investigated for their ability to inhibit the enzyme, presumably by interfering with association of the B1 and B2 subunits. AcYLVGQIDSE, corresponding by sequence homology to a nonapeptide that inhibits herpes simplex RNR shows no inhibition of the E. cole enzyme, whereas AcDDLSNFQL, the C-terminal octapeptide of the E. coli B2 subunit, is a noncompetitive inhibitor. Neither bradykinin (RPPGFSPER) nor the pentapeptide AcSNFQL inhibits the E. coli enzyme. Transferred nuclear Overhauser enhancement spectroscopy was used to probe the conformation of AcDDLSNFQL when it is bound to the B1 subunit. These experiments suggest that the peptide adopts a turn in the region of Asn{sub 5} and Phe{sub 6} and that a hydrophobic cluster of the phenylalanine and leucine side chains is involved in the interaction surface.

• OSTI ID: 5822309
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:33; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
BACTERIA
BIOCHEMICAL REACTION KINETICS
CARBOXYLIC ACIDS
ENZYME INHIBITORS
ENZYMES
ESCHERICHIA COLI
KINETICS
LEUCINE
MAGNETIC RESONANCE
MICROORGANISMS
NUCLEAR MAGNETIC RESONANCE
ORGANIC ACIDS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
OXIDOREDUCTASES
PEPTIDES
PHENYLALANINE
PROTEINS
REACTION KINETICS
RESONANCE