Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (LDH-M)

 LDHA_SQUAC              Reviewed;         333 AA.
P00341; Q92114;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
05-DEC-2018, entry version 126.
RecName: Full=L-lactate dehydrogenase A chain;
Short=LDH-A;
EC=1.1.1.27;
AltName: Full=LDH-M;
Name=ldha;
Squalus acanthias (Spiny dogfish).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
Elasmobranchii; Squalimorphii; Squaliformes; Squalidae; Squalus.
NCBI_TaxID=7797;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=8541980;
Stock D.W., Powers D.A.;
"The cDNA sequence of the lactate dehydrogenase-A of the spiny dogfish
(Squalus acanthias): corrections to the amino acid sequence and an
analysis of the phylogeny of vertebrate lactate dehydrogenases.";
Mol. Mar. Biol. Biotechnol. 4:284-294(1995).
[2]
PROTEIN SEQUENCE OF 2-333, AND ACETYLATION AT ALA-2.
PubMed=838743;
Taylor S.S.;
"Amino acid sequence of dogfish muscle lactate dehydrogenase.";
J. Biol. Chem. 252:1799-1806(1977).
[3]
X-RAY CRYSTALLOGRAPHY.
PubMed=4795361; DOI=10.1016/0006-291X(73)91398-3;
Adams M.J., Ford G.C., Liljas A., Rossmann M.G.;
"Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase.";
Biochem. Biophys. Res. Commun. 53:46-51(1973).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=197516; DOI=10.1073/pnas.74.7.2677;
Eventoff W., Rossmann M.G., Taylor S.S., Torff H.-J., Meyer H.,
Keil W., Kiltz H.-H.;
"Structural adaptations of lactate dehydrogenase isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 74:2677-2681(1977).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND
SUBSTRATE ANALOG.
PubMed=3430615; DOI=10.1016/0022-2836(87)90293-2;
Abad-Zapatero C., Griffith J.P., Sussman J.L., Rossmann M.G.;
"Refined crystal structure of dogfish M4 apo-lactate dehydrogenase.";
J. Mol. Biol. 198:445-467(1987).
-!- CATALYTIC ACTIVITY:
Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
EC=1.1.1.27;
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:3430615}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U38893; AAA91038.1; -; mRNA.
PIR; A00350; DEDFLM.
PDB; 1LDM; X-ray; 2.10 A; A=2-333.
PDB; 3LDH; X-ray; 3.00 A; A=4-333.
PDB; 6LDH; X-ray; 2.00 A; A=2-333.
PDB; 8LDH; X-ray; 2.80 A; A=2-333.
PDBsum; 1LDM; -.
PDBsum; 3LDH; -.
PDBsum; 6LDH; -.
PDBsum; 8LDH; -.
ProteinModelPortal; P00341; -.
SMR; P00341; -.
iPTMnet; P00341; -.
PRIDE; P00341; -.
HOVERGEN; HBG000462; -.
SABIO-RK; P00341; -.
UniPathway; UPA00554; UER00611.
EvolutionaryTrace; P00341; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; NAD;
Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:838743}.
CHAIN 2 333 L-lactate dehydrogenase A chain.
/FTId=PRO_0000168455.
NP_BIND 30 58 NAD. {ECO:0000269|PubMed:3430615}.
ACT_SITE 194 194 Proton acceptor.
BINDING 100 100 NAD. {ECO:0000269|PubMed:3430615}.
BINDING 107 107 Substrate. {ECO:0000250}.
BINDING 139 139 NAD or substrate. {ECO:0000250}.
BINDING 170 170 Substrate.
BINDING 249 249 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:838743}.
CONFLICT 124 124 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 184 184 S -> C (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 198 200 SVP -> VPS (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 206 211 NVAGVS -> WNA (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 222 222 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 226 227 EN -> QD (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 286 287 ND -> DN (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 297 298 DN -> ND (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 4 8 {ECO:0000244|PDB:6LDH}.
STRAND 21 27 {ECO:0000244|PDB:6LDH}.
HELIX 31 41 {ECO:0000244|PDB:6LDH}.
TURN 42 44 {ECO:0000244|PDB:6LDH}.
STRAND 47 52 {ECO:0000244|PDB:6LDH}.
HELIX 56 68 {ECO:0000244|PDB:6LDH}.
HELIX 69 72 {ECO:0000244|PDB:6LDH}.
STRAND 78 83 {ECO:0000244|PDB:6LDH}.
HELIX 84 87 {ECO:0000244|PDB:6LDH}.
STRAND 91 95 {ECO:0000244|PDB:6LDH}.
HELIX 107 128 {ECO:0000244|PDB:6LDH}.
STRAND 133 136 {ECO:0000244|PDB:6LDH}.
STRAND 138 140 {ECO:0000244|PDB:1LDM}.
HELIX 141 152 {ECO:0000244|PDB:6LDH}.
HELIX 156 158 {ECO:0000244|PDB:6LDH}.
STRAND 159 161 {ECO:0000244|PDB:6LDH}.
HELIX 165 179 {ECO:0000244|PDB:6LDH}.
TURN 183 185 {ECO:0000244|PDB:6LDH}.
STRAND 188 190 {ECO:0000244|PDB:3LDH}.
STRAND 192 195 {ECO:0000244|PDB:6LDH}.
HELIX 202 204 {ECO:0000244|PDB:6LDH}.
HELIX 215 218 {ECO:0000244|PDB:6LDH}.
STRAND 223 228 {ECO:0000244|PDB:6LDH}.
HELIX 230 246 {ECO:0000244|PDB:6LDH}.
HELIX 251 265 {ECO:0000244|PDB:6LDH}.
STRAND 270 277 {ECO:0000244|PDB:6LDH}.
STRAND 281 283 {ECO:0000244|PDB:6LDH}.
STRAND 289 297 {ECO:0000244|PDB:6LDH}.
STRAND 300 304 {ECO:0000244|PDB:6LDH}.
HELIX 311 327 {ECO:0000244|PDB:6LDH}.
SEQUENCE 333 AA; 36695 MW; 20C3B5F84B6C0117 CRC64;
MATLKDKLIG HLATSQEPRS YNKITVVGVG AVGMACAISI LMKDLADEVA LVDVMEDKLK
GEMMDLQHGS LFLHTAKIVS GKDYSVSAGS KLVVITAGAR QQEGESRLNL VQRNVNIFKF
IIPDIVKHSP DCIILVVSNP VDVLTYVAWK LSGLPMHRII GSGCNLDSAR FRYLMGERLG
VHSSSCHGWV IGEHGDSSVP VWSGMNVAGV SLKELHPELG TDKDKENWKK LHKDVVDSAY
EVIKLKGYTS WAIGLSVADL AETIMKNLCR VHPVSTMVKD FYGIKNDVFL SLPCVLDNHG
ISNIVKMKLK PDEEQQLQKS ATTLWDIQKD LKF


Related products :

Catalog number Product name Quantity
30-896 Lactate dehydrogenase C catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHC is testis-specific and belongs to the lactate dehydrogenase f 0.05 mg
U1698h CLIA DLD,Homo sapiens,Human,Lactate dehydrogenase D,LDHD,Probable D-lactate dehydrogenase, mitochondrial 96T
E1698h ELISA DLD,Homo sapiens,Human,Lactate dehydrogenase D,LDHD,Probable D-lactate dehydrogenase, mitochondrial 96T
DLDH-100 QuantiChrom™ Lactate Dehydrogenase Kit, Quantitative determination of lactate dehydrogenase LDH activity by colorimetric (565nm) method 100Tests
E1698h ELISA kit DLD,Homo sapiens,Human,Lactate dehydrogenase D,LDHD,Probable D-lactate dehydrogenase, mitochondrial 96T
E1698m ELISA DLD,Lactate dehydrogenase D,Ldhd,Mouse,Mus musculus,Probable D-lactate dehydrogenase, mitochondrial 96T
E1698m ELISA kit DLD,Lactate dehydrogenase D,Ldhd,Mouse,Mus musculus,Probable D-lactate dehydrogenase, mitochondrial 96T
U1698m CLIA DLD,Lactate dehydrogenase D,Ldhd,Mouse,Mus musculus,Probable D-lactate dehydrogenase, mitochondrial 96T
DLDH-100 QuantiChrom™ Lactate Dehydrogenase Kit, Quantitative determination of lactate dehydrogenase LDH activity by colorimetric (565nm) method. Procedure 30 min. Kit size 100 tests. Detection limit 2 U_L. 100tests
C236 L-Lactate Dehydrogenase B Chain LDH-B lmg
C235 L-Lactate Dehydrogenase A Chain LDH-A 500
C235 L-Lactate Dehydrogenase A Chain LDH-A lmg
C236 L-Lactate Dehydrogenase B Chain LDH-B 500
EH2155 L-lactate dehydrogenase A chain Elisa Kit 96T
ER648 L-lactate dehydrogenase C chain Elisa Kit 96T
ER646 L-lactate dehydrogenase A chain Elisa Kit 96T
EH2156 L-lactate dehydrogenase C chain Elisa Kit 96T
KN0424Ra Rat lactate dehydrogenase c chain Elisa kit 96 WELLS
ER647 L-lactate dehydrogenase B chain Elisa Kit 96T
C277 Human L-Lactate Dehydrogenase B Chain LDH-B l0
C277 Human L-Lactate Dehydrogenase A Chain LDH-A 50
C236 Human L-Lactate Dehydrogenase A Chain LDH-A l0
C148 Human L-Lactate Dehydrogenase B Chain LDH-B 50
CSB-RP013574h Recombinant human L-lactate dehydrogenase B chain 500ug
BPA1070 Lactate dehydrogenase B chain, LDH-B Polyclonal Antibodie 100 μg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur