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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1tph

E.C. nametriose-phosphate isomerase
SpeciesGallus gallus (Chicken)
E.C. Number (IntEnz) 5.3.1.1
CSA Homologues of 1tphThere are 112 Homologs
CSA Entries With UniProtID P00940
CSA Entries With EC Number 5.3.1.1
PDBe Entry 1tph
PDBSum Entry 1tph
MACiE Entry M0324

Literature Report

IntroductionTriosephosphate isomerase (TIM) is a glycolytic enzyme that catalyses the central reaction in the glycolytic pathway, the interconversion of D-glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). It is a homodimer and only the homodimer is fully active. TIM is known to exist in an unliganded and liganded conformation and the loop-6, in particular, would undergo the major conformational changes when there is a substrate or inhibitor bound at the active site. In addition, the shift of loop-6 preferentially stabilises the enediole phosphate intermediate.
MechansimGlu 165 acts as a general base to abstract the pro-R proton from C1 of DHAP, with electrophilic catalysis by His 95 and possibly also Asn 11 and Lys 13 serving to make the hydrogen more acidic and to stabilise the partial negative charge that forms on the carbonyl oxygen in the transition state. Formation of the cis-enediol intermediate is aided by His 95 also acting as a general acid to donate a proton to the substrate carbonyl oxygen. Then Glu 165 transfers a proton back to C2 of the intermediate to give GAP [2][5].
Reaction

Catalytic Sites for 1tph

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
Lys11313macie:sideChain
His19595macie:sideChain
Asn11111macie:sideChain
Glu1165165macie:sideChain
Gly1171171macie:mainChainAmide

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
Lys21313macie:sideChain
His29595macie:sideChain
Asn21111macie:sideChain
Glu2165165macie:sideChain
Gly2171171macie:mainChainAmide

Literature References

Notes:
Lolis E
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Biochemistry 1990 29 6609-6618
PubMed: 2204417
Lolis E
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Biochemistry 1990 29 6619-6625
PubMed: 2204418
Wierenga RK
Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase.
J Mol Biol 1992 224 1115-1126
PubMed: 1569570
Zhang Z
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
Biochemistry 1994 33 2830-2837
PubMed: 8130195
Knowles JR.
Enzyme catalysis: not different, just better.
Nature 1991 350 121-124
PubMed: 2005961
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