Claim · model-written summary
Comparison of b PFK amino acid sequences from a variety of organisms identified two critical Asp residues typical of the enzyme activity site and other binding sites.
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Verbatim
e0“A comparison between the amino acid sequences of b PFKs from a variety of organisms allowed us to identify the two critical Asp residues typical of this enzyme's activity site and the other binding sites; these residues are tightly conserved in all members of this protein family”
Title
J Suzuki; M A Mutton; M I T Ferro; et al. PubMed 2003
Other claims from this paper (6)
- Observation Both the alpha and beta subunits of PPi-PFK were identified in the sugar cane EST database using Citrus paradisi sequences.
- Observation The deduced amino acid sequence of the sugar cane alpha subunit showed 76% similarity to the C. paradisi alpha subunit.
- Observation The deduced amino acid sequence of the sugar cane beta subunit showed 80% similarity to the C. paradisi beta subunit.
- Observation The alpha and beta subunits are distinct subunits found at different concentrations in several sugar cane tissues.
- Observation These residues are tightly conserved in all members of the protein family.
- Observation There appear to be catalytic residues on the b subunit of the pyrophosphate-dependent enzyme.