Paper · 2003 · PubMed

Putative pyrophosphate phosphofructose 1-kinase genes identified in sugar cane may be getting energy from pyrophosphate.

J Suzuki; M A Mutton; M I T Ferro; et al.

7
claims
9
verbatim quotes
14
citations
2
research areas
✓
Open access · other-oa

Abstract

Pyrophosphate-dependent phosphofructokinase (PPi-PFK) has been detected in several types of plant cells, but the gene has not been reported in sugar cane. Using Citrus paradisi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have identified both the alpha and beta subunits of this enzyme. The deduced amino acid sequences showed 76 and 80% similarity with the corresponding alpha and beta subunits of C. paradisi. A high degree of similarity was also observed among the PFK b subunits when the alignment of the sugar cane sequences was compared to those of Ricinus communis and Solanum tuberosum. It appears that alpha and beta are two distinct subunits; they were found at different concentrations in several sugar cane tissues. It remains to be determined if the different gene expression levels have some physiological importance and how they affect sucrose synthesis, export, and storage in vacuoles. 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. Apparently, there are catalytic residues on the b subunit of the pyrophosphate-dependent enzyme.

Abstract from the paper’s OpenAlex record; open copy licensed other-oa. Read at the source ↗

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Claims 7

Observationobservedoriginal resultmeasured

Claim · model-written summary

Both the alpha and beta subunits of PPi-PFK were identified in the sugar cane EST database using Citrus paradisi sequences.

Taxon
sugar canee0
Gene
PPi-PFKe0
Outcome
identified both the alpha and beta subunitse0

Verbatim

e0

“Using Citrus paradisi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have identified both the alpha and beta subunits of this enzyme”

✓ located verbatim in the source · abstract, characters 155–329 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

The deduced amino acid sequence of the sugar cane alpha subunit showed 76% similarity to the C. paradisi alpha subunit.

Taxon
sugar canet0
Gene
alpha and beta subunitse0
Outcome
similaritye0
Value
76e0
Comparator
C. paradisie0

Verbatim

e0

“The deduced amino acid sequences showed 76 and 80% similarity with the corresponding alpha and beta subunits of C. paradisi”

✓ located verbatim in the source · abstract, characters 331–454 · show in text ↑
t0

“sugar cane”

✓ located verbatim in the source · title, characters 68–78 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

The deduced amino acid sequence of the sugar cane beta subunit showed 80% similarity to the C. paradisi beta subunit.

Taxon
sugar canet0
Gene
alpha and beta subunitse0
Outcome
similaritye0
Value
80%e0
Comparator
C. paradisie0

Verbatim

e0

“The deduced amino acid sequences showed 76 and 80% similarity with the corresponding alpha and beta subunits of C. paradisi”

✓ located verbatim in the source · abstract, characters 331–454 · show in text ↑
t0

“sugar cane”

✓ located verbatim in the source · title, characters 68–78 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

The alpha and beta subunits are distinct subunits found at different concentrations in several sugar cane tissues.

Taxon
sugar canee0
Organ / stage
several sugar cane tissuese0
Outcome
different concentrationse0

Verbatim

e0

“they were found at different concentrations in several sugar cane tissues”

✓ located verbatim in the source · abstract, characters 697–770 · show in text ↑
Observationobservedoriginal resultmeasured

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.

Taxon
a variety of organismse0
Gene
b PFKse0
Outcome
two critical Asp residuese0

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”

✓ located verbatim in the source · abstract, characters 947–1226 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

These residues are tightly conserved in all members of the protein family.

Taxon
a variety of organismse0
Gene
b PFKse0
Outcome
tightly conservede0

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”

✓ located verbatim in the source · abstract, characters 947–1226 · show in text ↑
Observationauthor interpretationoriginal resultmeasured

Claim · model-written summary

There appear to be catalytic residues on the b subunit of the pyrophosphate-dependent enzyme.

Outcome
catalytic residues on the b subunite0

Not reportedTaxon

Verbatim

e0

“Apparently, there are catalytic residues on the b subunit of the pyrophosphate-dependent enzyme”

✓ located verbatim in the source · abstract, characters 1228–1323 · show in text ↑