Serine transhydroxymethylase. Relaxation and transient kinetic study of the formation and interconversion of the enzyme-glycine complexes.

@article{Schirch1975SerineTR,
  title={Serine transhydroxymethylase. Relaxation and transient kinetic study of the formation and interconversion of the enzyme-glycine complexes.},
  author={L. Schirch},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 5},
  pages={
          1939-45
        }
}
  • L. Schirch
  • Published 1975 in The Journal of biological chemistry
Serine transhydroxymethylase forms three enzyme-glycine complexes which absorb at 3.43, 425, and 495 nm. Temperature-jump studies show three relaxations. Two of the relaxations are observed at both 343 and 425 nm but not at 495 nm. A slower third relaxation is observed only at 495 nm. The absorbance changes for the two relaxations observable at 343 and 425 nm are in opposite directions suggesting that these relaxations are both attributable to the inter conversion of enzyme speiies absorbing at… CONTINUE READING

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