Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.11
Description:Phosphopyruvate hydratase.
Alternative Name: Enolase.
2-phosphoglycerate dehydratase.
Prosite: PDOC00148;
PDB:
PDBScop
6BFZ 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500;
6BFY 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500;
5OHG 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500;
3H8A 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500;
2FYM 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500; 8029120; 8029121; 8041499; 8041500;
 » show all

Cath: 3.20.20.120; 3.30.390.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.11
BRENDA Enzyme Link: BRENDA 4.2.1.11
KEGG Enzyme Link: KEGG4.2.1.11
BioCyc Enzyme Link: BioCyc 4.2.1.11
ExPASy Enzyme Link: ExPASy4.2.1.11
EC2PDB Enzyme Link: EC2PDB 4.2.1.11
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.11
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.11
IntEnz Enzyme Link: IntEnz 4.2.1.11
MEDLINE Enzyme Link: MEDLINE 4.2.1.11
MSA:

4.2.1.11;

Phylogenetic Tree:

4.2.1.11;

Uniprot:
M-CSA:
RHEA:10164 2-phospho-D-glycerate = H2O + phosphoenolpyruvate
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH2;+0:4]-[OH;+0:5]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH2;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
pH dependence of the reaction catalyzed by yeast Mg-enolase.Vinarov DA, Nowak T1998 Oct 279790688
Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants.Poyner RR, Laughlin LT, Sowa GA, Reed GH1996 Feb 68634301
Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing.Schurig H, Rutkat K, Rachel R, Jaenicke R1995 Feb7757011
Mechanism of enolase: the crystal structure of enolase-Mg2(+)-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-A resolution.Lebioda L, Stec B1991 Mar 192007120
The catalytic Mn2+ sites in the enolase-inhibitor complex: crystallography, single-crystal EPR, and DFT calculations.Carmieli R, Larsen TM, Reed GH, Zein S, Neese F, Goldfarb D2007 Apr 1117367133
A PURIFICATION OF BREWERS' AND BAKERS' YEAST ENOLASE YIELDING A SINGLE ACTIVE COMPONENT.WESTHEAD EW, MCLAIN G1964 Aug14235523
The isolation and characterization of rabbit muscle enolase.HOLT A, WOLD F1961 Dec13908561
Reverse protonation is the key to general acid-base catalysis in enolase.Sims PA, Larsen TM, Poyner RR, Cleland WW, Reed GH2003 Jul 1512846578
Purification of native alpha-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic.Whiting GC, Evans JT, Patel S, Gillespie SH2002 Oct12435062