Derivation of Triose Phosphate Isomerase
From Proteopedia
Derivation
As mentioned above, 1HTI comes from Homo sapiens; the functional annotation is given at the end of this page. The followings are some homologies according to the BLAST results(http://www.uniprot.org/blast/). The configurations are:
<1>Matrix: blosum62 <2>Threshold: 10 <3>Filtered: false <4>Gapped: true <5>Maximum number of hits reported: 250 <6>Database: uniprotkb (Protein) generated for BLAST on Nov 2, 2010
Accession Entry_Name Organism GO IDs and terms D3DUS9 D3DUS9_HUMAN Homo sapiens 0005975 carbohydrate metabolic process
0006006 glucose metabolic process 0003824 catalytic activity 0004807 triose-phosphate isomerase activity 0005625 soluble fraction 0005634 nucleus
P60175 TPIS_PANTR Pan troglodytes 0006006 glucose metabolic process
0006094 gluconeogenesis 0003824 catalytic activity 0004807 triose-phosphate isomerase activity
P60174 TPIS_HUMAN Homo sapiens 0005975 carbohydrate metabolic process
0006006 glucose metabolic process 0003824 catalytic activity 0004807 triose-phosphate isomerase activity 0005625 soluble fraction 0005634 nucleus
P00939 TPIS_RABIT Oryctolagus cuniculus(Rabbit)0006006 glucose metabolic process
0006094 gluconeogenesis 0003824 catalytic activity 0004807 triose-phosphate isomerase activity
P15426 TPIS_MACMU Macaca mulatta 0006094 gluconeogenesis
0006096 glycolysis 0003824 catalytic activity 0004807 triose-phosphate isomerase activity ... ...
What's New~
"Triosephosphate isomerase (TIM) is a perfectly evolved enzyme...Researchers continue to use TIM as a study object for their research, both for computational enzyme mechanism studies as well as for experimental studies."
--R. K. Wierenga, E. G. Kapetaniou and R. Venkatesan, "Triosephosphate isomerase: a highly evolved biocatalyst", Cell Mol Life Sci. 2010 Dec
"In the present study, we theoretically assessed the effects of 20 point mutations detected previously in a region of the triose-phosphate
isomerase gene (tpi) of the protozoan Giardia duodenalis on the three-dimensional structure of the ‘wild-type’ protein (TPI)...the findings
provide support for the “neutral theory”, which contends that evolution at the molecular level is not solely shaped by “Darwinian selection
but also by random drift of selectively neutral or nearly neutral mutants”."
--Nolan MJ, Hofmann A, Jex AR, Gasser RB, "A theoretical study to establish the relationship between the three-dimensional structure of triose-phosphate isomerase of Giardia duodenalis and point mutations in the respective gene", Mol Cell Probes. 2010 Oct
GO Functional Annotation
as TRIOSEPHOSPHATE ISOMERASE(reference: http://www.pdb.org/pdb/explore/explore.do?structureId=1HTI)
(1) Cellular component:
GO_ID GO_term
0005625 soluble fraction
0005634 nucleus
0005829 cytosol
(2) Biological process:
GO_ID GO_term
0008152 metabolic process
0007275 multicellular organismal development
0009790 embryonic development
0005975 carbohydrate metabolic process
0008610 lipid biosynthetic process
0019682 glyceraldehyde-3-phosphate metabolic process
0006633 fatty acid biosynthetic process
0006006 glucose metabolic process
0006094 gluconeogenesis
0006096 glycolysis
0006098 pentose-phosphate shunt
(3) Biochemical function:
GO_ID GO_term
0003824 catalytic activity
0005515 protein binding
0016853 isomerase activity
0004807 triose-phosphate isomerase activity
(Created by Mengfei Cao)