Studies on the sub-units of triose phosphate isomerase

Burton, Pamela M.; Waley, S. G.

doi:10.1042/bj1070737

Cited by 19 publications

(19 citation statements)

References 17 publications

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“…Assuming that the subunits difTcr, three forms could exist: AA, BB and the hybrid AB. A correlation of peptide mapping data with amino acid composition has, however, indicated that rabbit muscle triose phosphate isomerase is composed of identical or very similar polypeptide chains [4]. This has led to an alternate proposal that the multiple froms may represent conformers [4], a term first advanced by Kaplan to designate enzymes which are believed to have the same primary structure and molecular weight but which exist in varying conformations [27].…”

Section: Subunit Structure and Multiple Formsmentioning

confidence: 99%

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The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme

Krietsch¹,

Pentchev²,

Klingenburg³

et al. 1970

Eur J Biochem

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Triose phosphate isomerase was isolated from brewer's yeast and rabbit liver and was obtained in crystalline form. Chemical, physical and kinetic properties were compared to rabbit muscle triose phosphate isomerase. The molecular weight of all three enzymes is in the range of 56000 to 60000. In dodecyl sulfate or as modified maleylated protein, the enzymes dissociate into two polypeptide chains each having a molecular weight in the range of 24000 to 29000. The rabbit muscle and liver enzymes appear to be indistinguishable in terms of their amino acid composition, electrophoretic mobility, kinetic properties, inhibition sensitivity, pH optimum, molecular weight and N‐terminal amino acid (alanine). The yeast enzyme, on the other hand, was found different in the following respects; it has a several fold lower content of sulfur amino acids, is highly resistant to inactivation through photooxidation as well as sulfhydryl and alkylating agents. Furthermore, it contains different N‐terminal amino acids (valine and alanine) and has kinetic properties differing from those of the rabbit enzymes. The crystalline liver and muscle enzymes could be resolved into three distinct electrophoretic forms in starch and polyacrylamide gels. The possible interpretation of the multiple forms in terms of hybrids or conformers is discussed.

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Section: Subunit Structure and Multiple Formsmentioning

confidence: 99%

“…Most studies were performed on rabbit muscle triose phosphate isomerase. This enzyme was shown to have a molecular weight of 60000 and evidence indicated it to be a dimer [4]. It has a Unusual Abbreviations.…”

mentioning

confidence: 99%

The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme

Krietsch¹,

Pentchev²,

Klingenburg³

et al. 1970

Eur J Biochem

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“…Triose phosphate isomerase is a dimer (Johnson & Waley, 1967;Burton & Waley, 1968b), of molecular weight about 53 000. When the enzyme refolds, enzymic activity is acquired as dimer is formed (Waley, 1973).…”

Section: Vol 179mentioning

confidence: 99%

Spectrophotometric studies on the interaction between triose phosphate isomerase and inhibitors

Jones¹,

Waley²

1979

Biochemical Journal

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The binding of ligands to chicken muscle triose phosphate isomerase was studied. Changes in u.v. absorbance of the enzyme were used to measure binding, and the dissociation constant was determined over a range of pH values. The ligands were 2-phosphoglycollate and rac-glycerol 3-phosphate (only the D-isomer, sn-glycerol 1-phosphate, binds appreciably). Non-linear regression was used to fit calculated curves to the experimental points and hence to compare different models. Both active sites in the dimeric enzyme probably bound 2-phosphoglycollate, without any interaction between the sites. The results of crystallographic analysis [Phillips, Rivers, Sternberg, Thornton & Wilson (1977) Biochem. Soc. Trans. 5,[642][643][644][645][646][647], and experiments on the 1H, 13C and 31P n.m.r. of enzyme or 2-phosphoglycollate were combined with the present results to provide the basis for a model in which binding depends on glutamic acid-165 being protonated and on the ligand being fully ionized; additionally, binding affects the ionization of one histidine residue (probably histidine-100). The binding of the glycerol 3-phosphate, on the other hand, was independent of pH over the range pH 6.5-8.5 but decreased at lower pH values. This is explained on a model in which the binding of the monoanion of the ligand is markedly affected by the protonation of a residue in the enzyme, but the binding of the dianion is only slightly affected by this ionization.

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“…The molecular weight of the polypeptide chains has been estimated as 26500 from polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate (Coulson et al, 1970;Norton et al, 1970). Structural work on the cysteine peptides is consistent with the presence of two identical polypeptide chains (Burton & Waley, 1968;Miller & Waley, 1971a). Triose phosphate isomerase from Bacillus stearothermophilus is also a dimer and the chains are much the same size as those of the muscle enzyme (Fahey et al, 1971).…”

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confidence: 64%

“…Lysine, arginine and glutamine were present in the tryptic digest; they were obtained from the later fractions from the Sephadex fractionation. Glutamine (which had the low mobility on electrophoresis at pH3.5 characteristic of free amino acids, and was neutral at pH 6.5) is the C-terminal amino acid of the protein (Burton & Waley, 1968;Norton et al, 1970;Miller & Waley, 1971a The accompanying paper (Furth et al, 1974) arginine-17 in the rabbit enzyme. There are, apart from these gaps, 32 differences between the chains: the extent of identity is 86%.…”

Section: Sequences Ofpeptidesmentioning

confidence: 99%

The tryptic peptides of rabbit muscle triose phosphate isomerase

Corran

Waley

1974

Biochemical Journal

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1. The peptides obtained by tryptic digestion of S-[14C]carboxymethylated rabbit muscle triose phosphate isomerase have been studied. 2. The first step in the fractionation of the tryptic digest was gel filtration on coupled columns of Sephadex G-25 and G-50. Further fractionation was carried out by paper electrophoresis and paper chromatography. 3. The digest contained 26 peptides and three free amino acids. The sizes of the peptides ranged from two to 29 residues. 4. The sequences of the peptides have been determined. 5. The length of the polypeptide chains is about 250 amino acid residues. 6. The variant sequences encountered were due to partial deamidation; this may be one of the reasons for multiple forms of the enzyme. 7. The chicken and rabbit enzymes are compared. 8. Detailed evidence for the sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50024 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1973) 131, 5.

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Studies on the sub-units of triose phosphate isomerase

Cited by 19 publications

References 17 publications

The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme

The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme

Spectrophotometric studies on the interaction between triose phosphate isomerase and inhibitors

The tryptic peptides of rabbit muscle triose phosphate isomerase

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