enolase, glycolytic/ gluconeogenic enzyme, universally conserved protein
function
enzyme in glycolysis/ gluconeogenesis
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.1|Glycolysis][category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.2|Gluconeogenesis][category|SW 3|Information processing] → [category|SW 3.2|RNA synthesis and degradation] → [category|SW 3.2.4|RNases] → [category|SW 3.2.4.5|Effectors of RNA degradation][category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.5|Phosphorylation on a Ser residue][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.6|Phosphorylation on a Thr residue][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.7|Phosphorylation on a Tyr residue][category|SW 6|Groups of genes] → [category|SW 6.5|Universally conserved proteins]Gene
Coordinates
3,476,555 → 3,477,847
Phenotypes of a mutant
no growth on LB, requires glucose and malate [Pubmed|23420519]essential according to Kobayashi et al. on LB [Pubmed|12682299]The protein
Catalyzed reaction/ biological activity
2-phospho-D-glycerate = phosphoenolpyruvate H2O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate H(2)OProtein family
enolase family (according to Swiss-Prot)Kinetic information
reversible Michaelis-Menten [Pubmed|25885][SW|Domains]
substrate binding domain (366–369)Modification
phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 [Pubmed|17218307,16493705,17726680][SW|Cofactors]
Mg2Effectors of protein activity
Inhibited by EDTA [Pubmed|25885]Structure
[PDB|4A3R] [Pubmed|22198292][PDB|1W6T] (from ''Streptococcus pneumoniae'') [Pubmed|15476816][SW|Localization]
cytoplasm [Pubmed|16479537,27708634]membrane associated [Pubmed|18763711]exported, this requires a long, unbent α-helix (from A108 to L126) [Pubmed|15003462,21856851]Additional information
Enolase is a [SW|moonlighting protein]. [Pubmed|19193632]There are indications that this enzyme is an octamer [Pubmed|25885][SW|universally conserved protein]extensive information on the structure and enzymatic properties of Eno can be found at [http://www.proteopedia.org/wiki/index.php/Enolase Proteopedia]belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]Expression and Regulation
Operons
genes
[gene|ADA6F2EDC7B18FDFFA47CC8C55BCDDE1B6821160|cggR]-[gene|EB6512177418B1601C6641FB2DEE99C2CD10E671|gapA]-[gene|ECF0F2E906BF94F509817752827CA189AFBE53FE|pgk]-[gene|0B5E910DC94463E34ABD393E3A8F20191E4A38B2|tpi]-[gene|C86FB523451AC172A20801829B717E5A5F914211|pgm]-[gene|67651D5D3122A89F57F9E7D49074C82A8990A277|eno]
description
[Pubmed|11489127]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|11489127], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]regulatory mechanism
[protein|ADA6F2EDC7B18FDFFA47CC8C55BCDDE1B6821160|CggR]: repression, [Pubmed|11489127], in [regulon|ADA6F2EDC7B18FDFFA47CC8C55BCDDE1B6821160|CggR regulon]regulation
expression induced by glycolytic intermediates ([protein|ADA6F2EDC7B18FDFFA47CC8C55BCDDE1B6821160|CggR]) [protein|ADA6F2EDC7B18FDFFA47CC8C55BCDDE1B6821160|CggR] [Pubmed|11489127]the mRNA is processed between [gene|ADA6F2EDC7B18FDFFA47CC8C55BCDDE1B6821160|cggR] and [gene|EB6512177418B1601C6641FB2DEE99C2CD10E671|gapA] by [protein|872CCB5A49C9000BD95E4B0472556D5F60F7D7A4|RNase Y], this requires the [protein|EE52DFA35B935E551871D079A9BE877DB2001A3B|YmcA]-[protein|6C9A092F38739A3759793EF8B496569CD02C2E3F|YlbF]-[protein|EBD15C174A03B7FCDFFE4C5DB5D86E93F1B9CAC4|YaaT] complex [Pubmed|29794222]view in new tabgenes
[gene|ECF0F2E906BF94F509817752827CA189AFBE53FE|pgk]-[gene|0B5E910DC94463E34ABD393E3A8F20191E4A38B2|tpi]-[gene|C86FB523451AC172A20801829B717E5A5F914211|pgm]-[gene|67651D5D3122A89F57F9E7D49074C82A8990A277|eno]
description
[Pubmed|11489127]
view in new tabBiological materials
Mutant
GP594 (''eno''::''cat''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GP599 (''eno''::''erm''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GP698 (''eno''-''[gene|C86FB523451AC172A20801829B717E5A5F914211|pgm]''::''cat''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]Expression vector
pGP1426 (expression of ''[gene|67651D5D3122A89F57F9E7D49074C82A8990A277|eno]'' in ''B. subtilis'', in [SW|pBQ200]), available in [SW|Jörg Stülke]'s labpGP1500 (expression of ''[gene|C86FB523451AC172A20801829B717E5A5F914211|pgm]'' and ''[gene|67651D5D3122A89F57F9E7D49074C82A8990A277|eno]'' in ''B. subtilis'', in [SW|pBQ200]), available in [SW|Jörg Stülke]'s labpGP563 (N-terminal His-tag, purification from ''E. coli'', in [SW|pWH844]), available in [SW|Jörg Stülke]'s lab, [pubmed|20389117]pGP1276 (N-terminal Strep-tag, purification from ''E. coli'', in [SW|pGP172]), available in [SW|Jörg Stülke]'s labpGP93 (N-terminal Strep-tag, purification from ''B. subtilis'', for [SW|SPINE], in [SW|pGP380]), available in [SW|Jörg Stülke]'s lab, [pubmed|19193632]GP1215 (chromosomal ''eno''-''Strep'' fusion, ''spc''), purification from ''B. subtilis'', for [SW|SPINE], available in [SW|Jörg Stülke]'s lablacZ fusion
see ''[gene|ECF0F2E906BF94F509817752827CA189AFBE53FE|pgk]GFP fusion
pHT315-yfp-eno, available in [SW|Mijakovic] labGP1700 (in [SW|pBP43]), expression of '' eno-GFP''::''spc'' under the native promoter, available in [SW|Jörg Stülke]'s lab [Pubmed|27708634]two-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s lab, [pubmed|19193632]FLAG-tag construct
GP1214 (spc, based on [SW|pGP1331]), available in [SW|Jörg Stülke]'s labAntibody
available in [SW|Jörg Stülke]'s labLabs working on this gene/protein
[SW|Jörg Stülke], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]References
Reviews
Subcellular localization of enolase
16479537,18763711,20497499,15003462,21856851,24642254,27708634 Other original publications
23420519,17726680,17218307,12850135,19193632,11489127,8021172,17505547,25885,20572937,15476816,9988532,21803996,22198292,15378759