Literature DB >> 16313562

Aedes aegypti phosphohexomutases and uridine diphosphate-hexose pyrophosphorylases: comparison of primary sequences, substrate specificities and temporal transcription.

N Kato1, C R Mueller, V Wessely, Q Lan, B M Christensen.   

Abstract

Phosphohexomutases reversibly catalyse the transfer of the phosphate group of a glycosyl phosphate between the C6 and C1 positions, and uridine diphosphate (UDP)-hexose pyrophosphorylases catalyse the synthesis of UDP-hexose from uridine triphosphate (UTP) and hexose-1-phosphate. Both enzyme families are essential for nucleoside diphosphate hexose biosynthesis and are therefore critical for various physiological functions in the midgut of mosquitoes after a blood meal. We cloned and sequenced three phosphohexomutase and two UDP-hexose pyrophosphorylase cDNAs from Aedes aegypti. The products of the cDNAs were expressed and substrate specificities were examined. Herein we describe Ae. aegypti phosphoglucomutase 1, phosphoglucomutase 2, phosphoacetylglucosamine mutase, UDP-glucose pyrophosphorylase, and UDP-N-acetylglucosamine pyrophosphorylase. Transcripts of the genes expressing the enzymes are constitutively present in all life stages and blood-feeding does not seem to influence transcript abundance.

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Year:  2005        PMID: 16313562     DOI: 10.1111/j.1365-2583.2005.00592.x

Source DB:  PubMed          Journal:  Insect Mol Biol        ISSN: 0962-1075            Impact factor:   3.585


  3 in total

1.  Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.

Authors:  Kyle M Stiers; Andrew G Muenks; Lesa J Beamer
Journal:  Adv Protein Chem Struct Biol       Date:  2017-05-17       Impact factor: 3.507

2.  Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens.

Authors:  Ritcha Mehra-Chaudhary; Jacob Mick; John J Tanner; Michael T Henzl; Lesa J Beamer
Journal:  Proteins       Date:  2011-01-18

3.  Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase.

Authors:  Giulia Bandini; Karina Mariño; M Lucia Sampaio Güther; Amy K Wernimont; Sabine Kuettel; Wei Qiu; Shamshad Afzal; Anna Kelner; Raymond Hui; Michael A J Ferguson
Journal:  Mol Microbiol       Date:  2012-07-12       Impact factor: 3.501

  3 in total

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