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Literature summary extracted from

  • Cui, Y.; Barford, J.P.; Renneberg, R.
    Amperometric trienzyme ATP biosensors based on the coimmobilization of salicylate hydroxylase, glucose-6-phosphate dehydrogenase, and hexokinase (2008), Sens. Actuators B Chem., B132, 1-4.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.14.13.1 analysis two types of amperometric ATP biosensors are developed by using the coimmobilization of salicylate hydroxylase (SHL, EC 1.14.13.1), glucose-6-phosphate dehydrogenase (G6PDH, EC 1.1.1.49), and hexokinase (HEX, EC 2.7.1.1) on a Clark-type oxygen electrode and on a screenprinted electrode. The principles of the determination schemes are as follows: HEX transfers the phosphate group from ATP to glucose to form glucose-6-phosphate. G6PDH catalyzes the specific dehydrogenation of glucose-6-phosphate by consuming NAD+. The product, NADH initiates the irreversible decarboxylation and hydroxylation of salicylate by SHL to consume dissolved oxygen and generate catechol. This results in a detectable signal on a Clark-type electrode due to the SHL-enzymatic consumption of oxygen, or a detectable signal on a screen-printed electrode due to the SHL-enzymatic generation of catechol in the measurement of ATP. Both sensors show high performance characteristics with broad detection ranges, short measuring times, and good specificities Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.1 Pseudomonas sp.
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Synonyms

EC Number Synonyms Comment Organism
1.14.13.1 SHL
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 Pseudomonas sp.