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Enolase (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)

 ENO_STRP6               Reviewed;         435 AA.
Q5XD01; P82479;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
26-FEB-2020, entry version 118.
RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=M6_Spy0577;
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=286636;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-946 / MGAS10394;
PubMed=15272401; DOI=10.1086/422697;
Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
"Progress toward characterization of the group A Streptococcus metagenome:
complete genome sequence of a macrolide-resistant serotype M6 strain.";
J. Infect. Dis. 190:727-738(2004).
[2]
PROTEIN SEQUENCE OF 2-10; 17-34; 106-140; 181-191; 197-224; 256-270;
313-331; 345-395 AND 408-413, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=JRS4 / Serotype M6;
Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
VanBogelen R.A.;
"Two-dimensional gel electrophoresis map of Streptococcus pyogenes
proteins.";
Submitted (MAY-2000) to UniProtKB.
[3]
PROTEIN SEQUENCE OF 2-51; 195-209 AND 367-372, FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBCELLULAR LOCATION, AND BINDING TO PLASMINOGEN.
STRAIN=D471 / Serotype M6;
PubMed=9603964; DOI=10.1074/jbc.273.23.14503;
Pancholi V., Fischetti V.A.;
"Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface
of pathogenic streptococci.";
J. Biol. Chem. 273:14503-14515(1998).
[4]
MUTAGENESIS OF LYS-428; LYS-434 AND LYS-435.
STRAIN=D471 / Serotype M6;
PubMed=14688086; DOI=10.1128/iai.72.1.94-105.2004;
Derbise A., Song Y.P., Parikh S., Fischetti V.A., Pancholi V.;
"Role of the C-terminal lysine residues of streptococcal surface enolase in
Glu- and Lys-plasminogen-binding activities of group A streptococci.";
Infect. Immun. 72:94-105(2004).
-!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
into phosphoenolpyruvate. It is essential for the degradation of
carbohydrates via glycolysis. Binds plasminogen when expressed on the
bacterial cell surface, potentially allowing the bacterium to acquire
surface-associated proteolytic activity, which in turn contributes to
tissue invasion and virulence. {ECO:0000255|HAMAP-Rule:MF_00318,
ECO:0000269|PubMed:9603964}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-
Rule:MF_00318};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
-!- ACTIVITY REGULATION: The covalent binding to the substrate causes
inactivation of the enzyme, and possibly serves as a signal for the
export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.49 mM for 2-phospho-D-glycerate {ECO:0000269|PubMed:9603964};
Vmax=31.25 mmol/min/mg enzyme {ECO:0000269|PubMed:9603964};
Note=Catalytically active also when expressed on the bacterial cell
surface.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
Rule:MF_00318}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318,
ECO:0000269|PubMed:9603964}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318,
ECO:0000269|PubMed:9603964}. Cell surface {ECO:0000255|HAMAP-
Rule:MF_00318, ECO:0000269|PubMed:9603964}. Note=Fractions of enolase
are present in both the cytoplasm and on the cell surface. The export
of enolase possibly depends on the covalent binding to the substrate;
once secreted, it remains attached to the cell surface.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
Rule:MF_00318}.
-!- SEQUENCE CAUTION:
Sequence=AAT86712.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; CP000003; AAT86712.1; ALT_FRAME; Genomic_DNA.
PDB; 3ZLF; X-ray; 2.15 A; A/B/C/D=1-435.
PDB; 3ZLG; X-ray; 2.10 A; A/B/C/D=1-435.
PDB; 3ZLH; X-ray; 2.90 A; A/B/C/D=1-435.
PDBsum; 3ZLF; -.
PDBsum; 3ZLG; -.
PDBsum; 3ZLH; -.
SMR; Q5XD01; -.
PRIDE; Q5XD01; -.
EnsemblBacteria; AAT86712; AAT86712; M6_Spy0577.
KEGG; spa:M6_Spy0577; -.
HOGENOM; CLU_031223_0_1_9; -.
KO; K01689; -.
SABIO-RK; Q5XD01; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000001167; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:CAFA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
Magnesium; Metal-binding; Secreted; Virulence.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:9603964, ECO:0000269|Ref.2"
CHAIN 2..435
/note="Enolase"
/id="PRO_0000133984"
REGION 371..374
/note="Substrate binding"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
ACT_SITE 205
/note="Proton donor"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
ACT_SITE 344
/note="Proton acceptor"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
METAL 243
/note="Magnesium"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
METAL 292
/note="Magnesium"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
METAL 319
/note="Magnesium"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
BINDING 155
/note="Substrate"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
BINDING 164
/note="Substrate"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
BINDING 292
/note="Substrate"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
BINDING 319
/note="Substrate"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
BINDING 344
/note="Substrate (covalent); in inhibited form"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
BINDING 395
/note="Substrate"
/evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SITE 428
/note="Important for binding of plasminogen"
SITE 434
/note="Important for binding of plasminogen"
SITE 435
/note="Important for binding of plasminogen"
MUTAGEN 428
/note="K->L: No effect on catalytic activity; significant
decrease in the ability to bind Glu- and Lys-plasminogen."
/evidence="ECO:0000269|PubMed:14688086"
MUTAGEN 434
/note="K->L: No effect on catalytic activity; significant
decrease in the ability to bind Glu- and Lys-plasminogen."
/evidence="ECO:0000269|PubMed:14688086"
MUTAGEN 435
/note="K->L: No effect on catalytic activity; significant
decrease in the ability to bind Glu- and Lys-plasminogen."
/evidence="ECO:0000269|PubMed:14688086"
CONFLICT 42
/note="S -> G (in Ref. 3; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 44
/note="G -> T (in Ref. 3; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 367
/note="T -> S (in Ref. 3; AA sequence)"
/evidence="ECO:0000305"
STRAND 3..13
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 19..27
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 32..36
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 44..47
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 59..61
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 65..73
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 75..79
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 87..98
/evidence="ECO:0000244|PDB:3ZLG"
TURN 104..106
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 108..126
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 130..135
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 144..151
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 153..155
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 157..159
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 163..168
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 175..195
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 215..228
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 237..243
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 246..249
/evidence="ECO:0000244|PDB:3ZLG"
TURN 252..255
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 256..258
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 260..263
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 272..285
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 288..293
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 300..310
/evidence="ECO:0000244|PDB:3ZLG"
TURN 311..313
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 314..319
/evidence="ECO:0000244|PDB:3ZLG"
TURN 320..324
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 326..334
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 339..343
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 345..348
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 351..363
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 367..371
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 381..388
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 393..395
/evidence="ECO:0000244|PDB:3ZLG"
STRAND 399..401
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 402..418
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 419..421
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 426..429
/evidence="ECO:0000244|PDB:3ZLG"
HELIX 431..433
/evidence="ECO:0000244|PDB:3ZLF"
SEQUENCE 435 AA; 47355 MW; 5E285F357966C572 CRC64;
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYL
GLGTQKAVDN VNNIIAKAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR
AAADYLEVPL YTYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMIMPV GAPTFKEGLR
WGAEVFHALK KILKERGLVT AVGDEGGFAP KFEGTEDGVE TILKAIEAAG YEAGENGIMI
GFDCASSEFY DKERKVYDYT KFEGEGAAVR TSAEQVDYLE ELVNKYPIIT IEDGMDENDW
DGWKVLTERL GKRVQLVGDD FFVTNTEYLA RGIKENAANS ILIKVNQIGT LTETFEAIEM
AKEAGYTAVV SHRSGETEDS TIADIAVATN AGQIKTGSLS RTDRIAKYNQ LLRIEDQLGE
VAQYKGIKSF YNLKK


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Related Genes :
[ENO2 LOS2 At2g36530 F1O11.16] Bifunctional enolase 2/transcriptional activator (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1)
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[ENO1 CAALFM_C108500CA CaO19.395 CaO19.8025] Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO1 ENO1L1 MBPB1 MPB1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein)
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[ENO2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
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[eno MSMEG_5415 MSMEI_5267] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON65_01250 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9Z23_21970 C9Z37_00915 C9Z43_06360 C9Z78_05610 CDC27_10055 CDL37_00765 CI694_25210 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DEN89_24995 DEO04_05510 DL800_09215 DQE83_22775 DTL43_21780 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E5P22_21380 E5S46_06650 EC95NR1_00961 ED648_25045 ELT20_21515 ELV08_24970 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 F7F11_20115 F7F29_22635 FNJ83_13175 FQ915_04255 FQR64_09390 FWK02_18105 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 QccE-14518] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[eno OR1_00408] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno CBP06_04475 E4195_23395 EQ845_16830] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR214_00082] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR37_00362] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR16_24200] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[yjeF nnrD nnrE A6V01_16625 AC789_1c45800 ACN002_4392 AW106_17115 BB545_04070 BN17_41441 BOH76_10905 BON72_19710 BON76_04155 BON95_14955 BTQ06_07255 BVL39_04290 C5N07_07145 C6669_06565 C7235_22665 C7B02_22745 C9162_14280 C9306_16010 C9Z28_08925 C9Z37_19300 C9Z69_17100 C9Z89_19770 CA593_04975 COD30_21525 CR538_23135 CRD98_04165 CRM83_17370 D0X26_12915 D2184_07750 D6T60_21965 D9J44_09440 D9K48_15185 DAH18_07435 DAH32_17635 DBQ99_23525 DEN97_13975 DEO19_11825 DIV22_15595 DL800_29085 DP277_02605 DQF57_15735 DS732_02620 E5S35_05440 ED600_08260 EHH55_18965 EJC75_20595 EKI52_12685 EYD11_20595 EYY78_08665 F1E03_05325 F7F23_18595 FQ915_09945] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BON76_21885 BvCmsC61A_00149 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C7B08_25495 C9Z39_20510 CR538_10415 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DJ503_24045 DP258_02540 E3B71_05970 EC3234A_36c00010 EC382_21100 ECTO6_01955 EHH55_07135 FORC82_1921 FV293_07100 NCTC8500_02249 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[eno BJD20_17165 CW311_11095] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno Loa_02648] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno1 eno ACTI_28410] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno E4195_02605] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[emp-7 NCU10042] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Embden-meyerhof pathway protein 7)
[nnrD nnrE BHS81_24940 BON75_25135 BUE81_24185 BW690_00535 C5P01_11605 C9114_00800 C9141_20385 C9160_20005 C9182_19515 C9201_17640 C9Z03_11025 C9Z39_09990 CG692_00180 CI641_014360 COD46_22200 CWS33_03515 D2185_07770 D3821_07085 D3O91_01535 D3Y67_00680 D9D20_08295 D9H68_15720 D9H94_06330 D9I18_04405 D9J11_13510 DAH30_09295 DAH34_17710 DAH37_06235 DEN89_23315 DEO04_15015 E0I42_01095 E2119_06500 E3B71_17555 E5P22_06605 EAI42_08035 EAI42_19730 EAI46_08330 EEP23_07485 EL75_3998 EL79_4176 EL80_4091 ELT20_09170 EPT01_09990 EXX24_09350 EXX78_19455 F1E13_09470 F1E19_03510 FQR64_20885 FRV13_14670 FV293_00830 RK56_012375] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]

Bibliography :
[32021984] Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study.
[32012501] Laboratory criteria of perinatal damage of central nervous system at premature newborns
[31825363] [The possibility of using neuron-specific enolase as a biomarker in the acute period of stroke].
[31690416] Expression of Neuroectodermal Markers in Atypical Fibromas in Two Dwarf Hamsters (Phodopus spp.).
[31690408] Oligodendroglioma with Neuronal Differentiation in Two Boxer Dogs.
[31671515] Neurofilament Heavy Chain and Tau Protein Are Not Elevated in Cerebrospinal Fluid of Adult Patients with Spinal Muscular Atrophy during Loading with Nusinersen.
[31639460] The crystal ball is filled with CSF.
[31638583] NSE & S100B protein blood level assessment during a long-distance trail race.
[31631606] [Application of a Radiomics Model for Preding Lymph Node Metastasis in Non-small Cell Lung Cancer].
[31623796] Comparative phosphoproteomic analysis of developing maize seeds suggests a pivotal role for enolase in promoting starch synthesis.