MDHC_TAESO
ID MDHC_TAESO Reviewed; 332 AA.
AC F1C7I4;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Malate dehydrogenase, cytoplasmic {ECO:0000303|PubMed:19277715};
DE EC=1.1.1.37 {ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955};
DE AltName: Full=Cytosolic malate dehydrogenase {ECO:0000303|PubMed:21439955, ECO:0000312|EMBL:ADX42057.1};
GN Name=MDH {ECO:0000303|PubMed:21439955, ECO:0000312|EMBL:ADX42057.1};
OS Taenia solium (Pork tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=6204;
RN [1] {ECO:0000312|EMBL:ADX42057.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=21439955; DOI=10.1016/j.exppara.2011.03.008;
RA Nava G., Laclette J.P., Bobes R., Carrero J.C., Reyes-Vivas H.,
RA Enriquez-Flores S., Mendoza-Hernandez G., Plancarte A.;
RT "Cloning, sequencing and functional expression of cytosolic malate
RT dehydrogenase from Taenia solium: Purification and characterization of the
RT recombinant enzyme.";
RL Exp. Parasitol. 128:217-224(2011).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND REACTION MECHANISM.
RX PubMed=19277715; DOI=10.1007/s00436-009-1380-6;
RA Plancarte A., Nava G., Mendoza-Hernandez G.;
RT "Purification, properties, and kinetic studies of cytoplasmic malate
RT dehydrogenase from Taenia solium cysticerci.";
RL Parasitol. Res. 105:175-183(2009).
CC -!- FUNCTION: Malate dehydrogenase. Has no activity with NADPH as
CC substrate. Does not show lactate dehydrogenase activity.
CC {ECO:0000269|PubMed:21439955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC Evidence={ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955};
CC -!- ACTIVITY REGULATION: By arsenate for both the forward and reverse
CC reactions. {ECO:0000269|PubMed:19277715}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for L-malate (at pH 9.6) {ECO:0000269|PubMed:21439955};
CC KM=42 uM for NAD (at pH 9.6) {ECO:0000269|PubMed:21439955};
CC KM=44 uM for oxaloacetate (at pH 8) {ECO:0000269|PubMed:21439955};
CC KM=167 uM for NADH (at pH 8) {ECO:0000269|PubMed:21439955};
CC KM=215 uM for L-malate (at pH 9.6) {ECO:0000269|PubMed:19277715};
CC KM=50 uM for NAD (at pH 9.6) {ECO:0000269|PubMed:19277715};
CC KM=2.4 uM for oxaloacetate (at pH 7.6) {ECO:0000269|PubMed:19277715};
CC KM=48 uM for NADH (at pH 7.6) {ECO:0000269|PubMed:19277715};
CC Vmax=77.03 umol/min/mg enzyme toward L-malate (at pH 9.6)
CC {ECO:0000269|PubMed:21439955};
CC Vmax=79.12 umol/min/mg enzyme toward NAD (at pH 9.6)
CC {ECO:0000269|PubMed:21439955};
CC Vmax=450.3 umol/min/mg enzyme toward oxaloacetate (at pH 8)
CC {ECO:0000269|PubMed:21439955};
CC Vmax=721.4 umol/min/mg enzyme toward NADH (at pH 8)
CC {ECO:0000269|PubMed:21439955};
CC Vmax=87.8 umol/min/mg enzyme toward L-malate (at pH 9.6)
CC {ECO:0000269|PubMed:19277715};
CC Vmax=104 umol/min/mg enzyme toward NAD (at pH 9.6)
CC {ECO:0000269|PubMed:19277715};
CC Vmax=1490 umol/min/mg enzyme toward oxaloacetate (at pH 7.6)
CC {ECO:0000269|PubMed:19277715};
CC Vmax=1714 umol/min/mg enzyme toward NADH (at pH 7.6)
CC {ECO:0000269|PubMed:19277715};
CC Note=kcat is 47.4 sec(-1) for L-malate. kcat is 385.6 sec(-1) for
CC NAD. kcat is 665.34 sec(-1) for oxaloacetate. kcat is 962.66 sec(-1)
CC for NADH. {ECO:0000269|PubMed:21439955};
CC pH dependence:
CC Optimum pH is 7.6 for oxaloacetate reduction and 9.6 for malate
CC oxidation (PubMed:21439955, PubMed:19277715). Stable between pH 6.8-
CC 8.5 for the forward reaction (PubMed:19277715).
CC {ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955};
CC Temperature dependence:
CC Has highest activity between 5-40 degrees Celsius. No activity at 60
CC degrees Celsius. {ECO:0000269|PubMed:21439955};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19277715}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19277715}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|RuleBase:RU003369, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ207526; ADX42057.1; -; Genomic_DNA.
DR AlphaFoldDB; F1C7I4; -.
DR SMR; F1C7I4; -.
DR BRENDA; 1.1.1.37; 7956.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01336; MDH_cytoplasmic_cytosolic; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR011274; Malate_DH_NAD-dep_euk.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19277715"
FT CHAIN 2..332
FT /note="Malate dehydrogenase, cytoplasmic"
FT /id="PRO_0000438645"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000102-1"
FT BINDING 11..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 129..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
SQ SEQUENCE 332 AA; 36517 MW; 83B104F5E1A7A3F1 CRC64;
MPGPLRVLIT GAAGQIAYNL SNMVANGNLF GKDQKIILHL LDIPEAKTVL EGVVMELQDC
AFTVLEGIVP THCLKEAFTD IDVALMVGAM PRKQGMERRD LLSSNVKIFK DQGEALEKYA
KKTVKVLVVG NPANTNCLIM SKYAPSIPKE NFTALSRLDH NRAIYQVAAK VGVPSECVKN
VCIWGNHSNK QFPDLAHAVV TKGGKQHPAK ELINDEKWVK EVFTPCVQNR GAAVIGLRKL
SSAASAAKAI VDQMHDWWFG TKEGEWVSMS VYSTGEHYGA PKDIYFSFPV TIKNGHYKVV
DGLAMDEWGK GLFKITADEL VDEREVALSS FK
