1988FEBS LettersOpen access

A novel pyrophosphate fructose‐6‐phosphate 1‐phosphotransferase from carrot roots Relation to PFK from the same source

Joshua Wong, Taewook Kang, Bob B. Buchanan

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Abstract

A novel type of pyrophosphate fructose‐6‐phosphate 1‐phosphotransferase (PFP) has been purified from carrot roots. The enzyme differs from its counterpart studied from other sources in subunit composition, response to regulatory metabolites and kinetic parameters. The properties of the enzyme are in accord with its function in a tissue that stores substantial quantities of sucrose. In describing the carrot root PFP, we have systematically compared its properties to those of phosphofructokinase from the same tissue. The results support the conclusion that, despite noteworthy similarities, the two enzymes are independent proteins, unlikely to undergo interconversion.

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A novel type of pyrophosphate fructose‐6‐phosphate 1‐phosphotransferase (PFP) has been purified from carrot roots. The enzyme differs from its counterpart studied from other sources in subunit composition, response to regulatory metabolites and kinetic parameters. The properties of the enzyme are in accord with its function in a tissue that stores substantial quantities of sucrose. In describing the carrot root PFP, we have systematically compared its properties to those of phosphofructokinase from the same tissue. The results support the conclusion that, despite noteworthy similarities, the two enzymes are independent proteins, unlikely to undergo interconversion.

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Available abstract

A novel type of pyrophosphate fructose‐6‐phosphate 1‐phosphotransferase (PFP) has been purified from carrot roots. The enzyme differs from its counterpart studied from other sources in subunit composition, response to regulatory metabolites and kinetic parameters. The properties of the enzyme are in accord with its function in a tissue that stores substantial quantities of sucrose. In describing the carrot root PFP, we have systematically compared its properties to those of phosphofructokinase from the same tissue. The results support the conclusion that, despite noteworthy similarities, the two enzymes are independent proteins, unlikely to undergo interconversion.

Key concepts: Phosphofructokinase, Phosphotransferase, Pyrophosphate, Biochemistry, Enzyme, Fructose, Chemistry, Protein subunit

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