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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Drosophila melanogaster

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Drosophila melanogaster
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
triosephosphate isomerase, triose phosphate isomerase, triose-phosphate isomerase, tctim, pftim, gltim, monotim, pfutim, cp 25, cytoplasmic tpi, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CP 25
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D-glyceraldehyde-3-phosphate ketol-isomerase
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Isomerase, triose phosphate
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Lactacin B inducer protein
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monoTIM
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PfTIM
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Phosphotriose isomerase
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TIM
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Triose phosphate isomerase
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Triose phosphate mutase
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Triose phosphoisomerase
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Triosephosphate isomerase
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Triosephosphate mutase
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vTIM
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-78-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPIS_DROME
247
0
26626
Swiss-Prot
other Location (Reliability: 2)
K7Z7Z8_DROME
162
0
17406
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26500
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2 * 26500, SDS-PAGE, both wild-type and mutant M80T
53000
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gel filtration, both wild-type and mutant M80T
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 26500, SDS-PAGE, both wild-type and mutant M80T
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M80T
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analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis
additional information
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mutation wasted away is a recessive, hypomorphic mutation that causes progressive motor impairment, vacuolar neuropthology, and severely reduced lifespan. Mutation affects the gene for triosephosphate isomerase. There is no genetic evidence that the mutation leads to misfolded or aberrant protein. Mutation may lead to an accumulation of methylglyoxal and the consequent enhanced production of advanced glycation end products
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gnerer, J.P.; Kreber, R.A.; Ganetzky, B.
wasted away, a Drosophila mutation in triosephosphate isomerase, causes paralysis, neurodegeneration, and early death
Proc. Natl. Acad. Sci. USA
103
14987-14993
2006
Drosophila melanogaster
Manually annotated by BRENDA team
Seigle, J.L.; Celotto, A.M.; Palladino, M.J.
Degradation of functional triose phosphate isomerase protein underlies sugarkill pathology
Genetics
179
855-862
2008
Drosophila melanogaster
Manually annotated by BRENDA team