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Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus.
The entire amino acid sequence of the protein subunit of phosphofructokinase from Bacillus stearothermophilus has been established mainly by sequence analysis of cyanogen bromide fragments and of peptides derived from these fragments by further digestion with proteolytic enzymes. Overlaps of the cyanogen bromide fragments as well as peptide sequences necessary to complement and to confirm tentative assignments within the larger peptide fragments were obtained from the sequences of selected peptides isolated from tryptic and chymotryptic digests of the intact S-[14C]-carboxymethylated protein. Sequence information was also provided by automated sequence analysis of the intact protein subunit and of some of the larger peptide fragments. The sequence is as follows: (See Text).
PMID: 6447595 [PubMed - indexed for MEDLINE]
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Cited by 5 PubMed Central articles
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Time-resolved fluorescence of the single tryptophan of Bacillus stearothermophilus phosphofructokinase.
Kim SJ, Chowdhury FN, Stryjewski W, Younathan ES, Russo PS, Barkley MD.
Biophys J. 1993 Jul; 65(1):215-26.
[Biophys J. 1993]
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The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP.
Auzat I, Le Bras G, Garel JR.
Proc Natl Acad Sci U S A. 1994 Jun 7; 91(12):5242-6.
[Proc Natl Acad Sci U S A. 1994]
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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.
Walker JE, Saraste M, Runswick MJ, Gay NJ.
EMBO J. 1982; 1(8):945-51.
[EMBO J. 1982]
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