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Biomedical subjects

T E Creighton

Publications and source records attributed to T E Creighton.

At least 127 records · Page 7Linked to original sources
PubMed1978

[52-Homoserine]-basic pancreatic trypsin inhibitor. Preparation and properties of a protein analog.

Treatment of basic pancreatic trypsin inhibitor (BPTI) with cyanogen bromide smoothly cleaves the polypeptide chain at the single methionyl residue. The newly formed homoserine lactone and alpha-amino functions are held in proximity by a disulfide linkage, and in neutral aqueous solution react together spontaneously to re-form the peptide chain. The resulting analog, [52-homoserine]-BPTI is very similar to the native molecule in most properties measured. The rate of formation of this analog from the chain-cleaved intermediate has been determined. It is apparent that the facility of analog synthesis is due in large part to the retention of the native protein conformation in the cyanogen bromide-cleaved intermediate.

Amino Acid Sequence↗
PubMed1970

N-(5'-phosphoribosyl)anthranilate isomerase-indol-3-ylglycerol phosphate synthetase of tryptophan biosynthesis. Relationship between the two activities of the enzyme from Escherichia coli.

Further evidence is presented to confirm the previous conclusion that the enzyme from Escherichia coli catalysing the two sequential reactions in tryptophan biosynthesis, N-(5'-phosphoribosyl)anthranilic acid (PRA) --> 1-(o-carboxyphenyl-amino)-1-deoxyribulose 5-phosphate (CdRP) --> indol-3-ylglycerol phosphate (InGP)+CO(2)+H(2)O, consists of a single polypeptide chain. The kinetic properties of the enzyme demonstrate that intermediate CdRP formed from PRA must dissociate from the enzyme before it can be converted into InGP. It is concluded that there are two distinct and non-overlapping catalytic sites on the enzyme for the two reactions. The expected complementation between a mutationally altered form of the enzyme lacking the first reaction and a mutationally altered form lacking the second reaction has been demonstrated in vitro by InGP formation from PRA. This system thus exhibits intracistronic complementation with a non-oligomeric protein gene product.

Amino Sugars↗