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Phenylalanine racemase (ATP-hydrolysing)


FieldValue
NamePhenylalanine racemase (ATP-hydrolysing)
EC_number5.1.1.11
CAS_number37290-95-2
image1amu.png
captionPhenylalanine Racemase(ATP Hydrolysing), image from Protein Data Bank

The enzyme phenylalanine racemase (, phenylalanine racemase, phenylalanine racemase (adenosine triphosphate-hydrolysing), gramicidin S synthetase I) is the enzyme that acts on amino acids and derivatives. It activates both the L & D stereo isomers of phenylalanine to form L-phenylalanyl adenylate and D-phenylalanyl adenylate, which are bound to the enzyme. These bound compounds are then transferred to the thiol group of the enzyme followed by conversion of its configuration, the D-isomer being the more favorable configuration of the two, with a 7 to 3 ratio between the two isomers. The racemisation reaction of phenylalanine is coupled with the highly favorable hydrolysis of adenosine triphosphate (ATP) to adenosine monophosphate (AMP) and pyrophosphate (PP), thermodynamically allowing it to proceed. This reaction is then drawn forward by further hydrolyzing PP to inorganic phosphate (Pi), via Le Chatelier's principle.

Other names

  • phenylalanine racemase
  • phenylalanine racemase (adenosine triphosphate-hydrolysing)
  • gramicidin S synthetase I

Pathway

  • Phenylalanine Metabolism

Substrate

  • L – Phenylalanine

Product

  • D - Phenylalanine

Cofactor

  • Pyridoxal-phosphate (active form of vitamin B6)

Quick facts

  • pH Range = 7.2 – 8.6
  • Equilibrium Ratio: L-Phe:D-Phe = 3:7
  • Specific Activity: 0.019

The reaction

|reaction_direction_(forward/reversible/reverse)=forward |minor_forward_substrate(s)=ATP |minor_forward_product(s)=AMP+PP |minor_reverse_substrate(s)= |minor_reverse_product(s)= |}

References

Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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