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P23368

- MAOM_HUMAN

UniProt

P23368 - MAOM_HUMAN

Protein

NAD-dependent malic enzyme, mitochondrial

Gene

ME2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate + NAD+ = pyruvate + CO2 + NADH.
    Oxaloacetate = pyruvate + CO2.

    Cofactori

    Divalent metal cations. Prefers magnesium or manganese.

    Enzyme regulationi

    Subject to allosteric activation by fumarate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei67 – 671Allosteric activator2 Publications
    Binding sitei91 – 911Allosteric activator2 Publications
    Active sitei112 – 1121Proton donor
    Binding sitei165 – 1651Substrate1 Publication
    Active sitei183 – 1831Proton acceptor
    Metal bindingi255 – 2551Divalent metal cation
    Metal bindingi256 – 2561Divalent metal cation
    Binding sitei259 – 2591NAD2 Publications
    Metal bindingi279 – 2791Divalent metal cation
    Sitei279 – 2791Important for activityBy similarity
    Binding sitei421 – 4211Substrate1 Publication
    Binding sitei466 – 4661Substrate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1739NAD2 Publications
    Nucleotide bindingi311 – 32818NAD2 PublicationsAdd
    BLAST

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. malate dehydrogenase (decarboxylating) (NAD+) activity Source: ProtInc
    3. metal ion binding Source: UniProtKB-KW
    4. NAD binding Source: InterPro
    5. oxaloacetate decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. malate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD

    Enzyme and pathway databases

    SABIO-RKP23368.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-dependent malic enzyme, mitochondrial (EC:1.1.1.38)
    Short name:
    NAD-ME
    Alternative name(s):
    Malic enzyme 2
    Gene namesi
    Name:ME2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6984. ME2.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671R → S: Abolishes activation by fumarate. 1 Publication
    Mutagenesisi91 – 911R → T: Abolishes activation by fumarate. 1 Publication

    Organism-specific databases

    PharmGKBiPA30724.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1818Mitochondrion1 PublicationAdd
    BLAST
    Chaini19 – 584566NAD-dependent malic enzyme, mitochondrialPRO_0000018537Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei156 – 1561N6-acetyllysine1 Publication
    Modified residuei224 – 2241N6-acetyllysine1 Publication
    Modified residuei240 – 2401N6-acetyllysine1 Publication
    Modified residuei272 – 2721N6-acetyllysine1 Publication
    Modified residuei346 – 3461N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP23368.
    PaxDbiP23368.
    PeptideAtlasiP23368.
    PRIDEiP23368.

    PTM databases

    PhosphoSiteiP23368.

    Expressioni

    Gene expression databases

    BgeeiP23368.
    CleanExiHS_ME2.
    GenevestigatoriP23368.

    Organism-specific databases

    HPAiHPA008247.
    HPA008880.

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Protein-protein interaction databases

    BioGridi110364. 3 interactions.
    IntActiP23368. 1 interaction.
    MINTiMINT-4530114.
    STRINGi9606.ENSP00000321070.

    Structurei

    Secondary structure

    1
    584
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 304
    Turni32 – 343
    Helixi37 – 393
    Helixi42 – 476
    Turni51 – 533
    Helixi61 – 7414
    Helixi78 – 8912
    Helixi93 – 10210
    Helixi104 – 1118
    Helixi115 – 1217
    Helixi123 – 1264
    Beta strandi132 – 1365
    Helixi137 – 1393
    Turni140 – 1423
    Helixi143 – 1475
    Beta strandi157 – 1615
    Beta strandi163 – 1653
    Turni167 – 1693
    Helixi173 – 1775
    Helixi178 – 19114
    Helixi195 – 1973
    Beta strandi198 – 2058
    Helixi212 – 2143
    Helixi229 – 24618
    Beta strandi251 – 2544
    Helixi259 – 26911
    Turni270 – 2723
    Beta strandi273 – 2775
    Helixi278 – 29821
    Helixi302 – 3043
    Beta strandi307 – 3104
    Helixi314 – 32916
    Helixi334 – 3396
    Beta strandi341 – 3455
    Turni360 – 3623
    Helixi363 – 3653
    Helixi377 – 3848
    Beta strandi387 – 3915
    Beta strandi394 – 3963
    Helixi401 – 41010
    Beta strandi415 – 4184
    Helixi423 – 4253
    Beta strandi426 – 4283
    Helixi430 – 4367
    Turni437 – 4393
    Beta strandi442 – 4476
    Helixi467 – 4693
    Helixi471 – 48010
    Helixi488 – 49912
    Helixi504 – 5085
    Helixi516 – 5183
    Helixi519 – 53618
    Helixi549 – 5557

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DO8X-ray2.20A/B/C/D21-584[»]
    1EFKX-ray2.60A/B/C/D1-584[»]
    1EFLX-ray2.60A/B/C/D1-584[»]
    1GZ3X-ray2.30A/B/C/D20-573[»]
    1GZ4X-ray2.20A/B/C/D23-573[»]
    1PJ2X-ray2.30A/B/C/D21-584[»]
    1PJ3X-ray2.10A/B/C/D21-584[»]
    1PJ4X-ray2.30A/B/C/D21-584[»]
    1PJLX-ray2.90A/B/C/D/E/F/G/H1-584[»]
    1QR6X-ray2.10A/B1-584[»]
    ProteinModelPortaliP23368.
    SMRiP23368. Positions 21-573.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23368.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the malic enzymes family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0281.
    HOGENOMiHOG000042486.
    HOVERGENiHBG000746.
    InParanoidiP23368.
    KOiK00027.
    OMAiLPDMYEW.
    OrthoDBiEOG7G4QF0.
    PhylomeDBiP23368.
    TreeFamiTF300537.

    Family and domain databases

    Gene3Di3.40.50.10380. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR015884. Malic_enzyme_CS.
    IPR012301. Malic_N_dom.
    IPR012302. Malic_NAD-bd.
    IPR001891. Malic_OxRdtase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00390. malic. 1 hit.
    PF03949. Malic_M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000106. ME. 1 hit.
    PRINTSiPR00072. MALOXRDTASE.
    SMARTiSM00919. Malic_M. 1 hit.
    [Graphical view]
    PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23368-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLSRLRVVST TCTLACRHLH IKEKGKPLML NPRTNKGMAF TLQERQMLGL    50
    QGLLPPKIET QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL 100
    QDDIESLMPI VYTPTVGLAC SQYGHIFRRP KGLFISISDR GHVRSIVDNW 150
    PENHVKAVVV TDGERILGLG DLGVYGMGIP VGKLCLYTAC AGIRPDRCLP 200
    VCIDVGTDNI ALLKDPFYMG LYQKRDRTQQ YDDLIDEFMK AITDRYGRNT 250
    LIQFEDFGNH NAFRFLRKYR EKYCTFNDDI QGTAAVALAG LLAAQKVISK 300
    PISEHKILFL GAGEAALGIA NLIVMSMVEN GLSEQEAQKK IWMFDKYGLL 350
    VKGRKAKIDS YQEPFTHSAP ESIPDTFEDA VNILKPSTII GVAGAGRLFT 400
    PDVIRAMASI NERPVIFALS NPTAQAECTA EEAYTLTEGR CLFASGSPFG 450
    PVKLTDGRVF TPGQGNNVYI FPGVALAVIL CNTRHISDSV FLEAAKALTS 500
    QLTDEELAQG RLYPPLANIQ EVSINIAIKV TEYLYANKMA FRYPEPEDKA 550
    KYVKERTWRS EYDSLLPDVY EWPESASSPP VITE 584
    Length:584
    Mass (Da):65,444
    Last modified:November 1, 1991 - v1
    Checksum:i4CEF9AF89B07D93D
    GO
    Isoform 2 (identifier: P23368-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         474-584: VALAVILCNT...SASSPPVITE → YRIPIC

    Note: No experimental confirmation available.

    Show »
    Length:479
    Mass (Da):53,586
    Checksum:i8F4D1C728EDD83E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti263 – 2631F → Y in BAG36189. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141P → L.
    Corresponds to variant rs16952692 [ dbSNP | Ensembl ].
    VAR_034104
    Natural varianti450 – 4501G → E.
    Corresponds to variant rs649224 [ dbSNP | Ensembl ].
    VAR_050017

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei474 – 584111VALAV…PVITE → YRIPIC in isoform 2. 1 PublicationVSP_042717Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55905 mRNA. Translation: AAA36197.1.
    AB045122 Genomic DNA. Translation: BAB40980.1.
    AK313391 mRNA. Translation: BAG36189.1.
    AC015864 Genomic DNA. No translation available.
    AC087687 Genomic DNA. No translation available.
    CH471096 Genomic DNA. Translation: EAW62980.1.
    BC000147 mRNA. Translation: AAH00147.1.
    AJ294818 mRNA. Translation: CAC14574.1.
    CCDSiCCDS11948.1. [P23368-1]
    CCDS54187.1. [P23368-2]
    PIRiA39503.
    RefSeqiNP_001161807.1. NM_001168335.1. [P23368-2]
    NP_002387.1. NM_002396.4. [P23368-1]
    UniGeneiHs.233119.

    Genome annotation databases

    EnsembliENST00000321341; ENSP00000321070; ENSG00000082212. [P23368-1]
    ENST00000382927; ENSP00000372384; ENSG00000082212. [P23368-2]
    GeneIDi4200.
    KEGGihsa:4200.
    UCSCiuc002ley.3. human. [P23368-1]
    uc010dpd.3. human. [P23368-2]

    Polymorphism databases

    DMDMi126733.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55905 mRNA. Translation: AAA36197.1 .
    AB045122 Genomic DNA. Translation: BAB40980.1 .
    AK313391 mRNA. Translation: BAG36189.1 .
    AC015864 Genomic DNA. No translation available.
    AC087687 Genomic DNA. No translation available.
    CH471096 Genomic DNA. Translation: EAW62980.1 .
    BC000147 mRNA. Translation: AAH00147.1 .
    AJ294818 mRNA. Translation: CAC14574.1 .
    CCDSi CCDS11948.1. [P23368-1 ]
    CCDS54187.1. [P23368-2 ]
    PIRi A39503.
    RefSeqi NP_001161807.1. NM_001168335.1. [P23368-2 ]
    NP_002387.1. NM_002396.4. [P23368-1 ]
    UniGenei Hs.233119.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DO8 X-ray 2.20 A/B/C/D 21-584 [» ]
    1EFK X-ray 2.60 A/B/C/D 1-584 [» ]
    1EFL X-ray 2.60 A/B/C/D 1-584 [» ]
    1GZ3 X-ray 2.30 A/B/C/D 20-573 [» ]
    1GZ4 X-ray 2.20 A/B/C/D 23-573 [» ]
    1PJ2 X-ray 2.30 A/B/C/D 21-584 [» ]
    1PJ3 X-ray 2.10 A/B/C/D 21-584 [» ]
    1PJ4 X-ray 2.30 A/B/C/D 21-584 [» ]
    1PJL X-ray 2.90 A/B/C/D/E/F/G/H 1-584 [» ]
    1QR6 X-ray 2.10 A/B 1-584 [» ]
    ProteinModelPortali P23368.
    SMRi P23368. Positions 21-573.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110364. 3 interactions.
    IntActi P23368. 1 interaction.
    MINTi MINT-4530114.
    STRINGi 9606.ENSP00000321070.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P23368.

    Polymorphism databases

    DMDMi 126733.

    Proteomic databases

    MaxQBi P23368.
    PaxDbi P23368.
    PeptideAtlasi P23368.
    PRIDEi P23368.

    Protocols and materials databases

    DNASUi 4200.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321341 ; ENSP00000321070 ; ENSG00000082212 . [P23368-1 ]
    ENST00000382927 ; ENSP00000372384 ; ENSG00000082212 . [P23368-2 ]
    GeneIDi 4200.
    KEGGi hsa:4200.
    UCSCi uc002ley.3. human. [P23368-1 ]
    uc010dpd.3. human. [P23368-2 ]

    Organism-specific databases

    CTDi 4200.
    GeneCardsi GC18P048405.
    HGNCi HGNC:6984. ME2.
    HPAi HPA008247.
    HPA008880.
    MIMi 154270. gene.
    neXtProti NX_P23368.
    PharmGKBi PA30724.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0281.
    HOGENOMi HOG000042486.
    HOVERGENi HBG000746.
    InParanoidi P23368.
    KOi K00027.
    OMAi LPDMYEW.
    OrthoDBi EOG7G4QF0.
    PhylomeDBi P23368.
    TreeFami TF300537.

    Enzyme and pathway databases

    SABIO-RK P23368.

    Miscellaneous databases

    EvolutionaryTracei P23368.
    GeneWikii ME2.
    ME2_(gene).
    GenomeRNAii 4200.
    NextBioi 16554.
    PROi P23368.
    SOURCEi Search...

    Gene expression databases

    Bgeei P23368.
    CleanExi HS_ME2.
    Genevestigatori P23368.

    Family and domain databases

    Gene3Di 3.40.50.10380. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR015884. Malic_enzyme_CS.
    IPR012301. Malic_N_dom.
    IPR012302. Malic_NAD-bd.
    IPR001891. Malic_OxRdtase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00390. malic. 1 hit.
    PF03949. Malic_M. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000106. ME. 1 hit.
    PRINTSi PR00072. MALOXRDTASE.
    SMARTi SM00919. Malic_M. 1 hit.
    [Graphical view ]
    PROSITEi PS00331. MALIC_ENZYMES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli."
      Loeber G., Infante A.A., Maurer-Fogy I., Krystek E., Dworkin M.B.
      J. Biol. Chem. 266:3016-3021(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Physical and transcriptional map of a 311-kb segment of chromosome 18q21, a candidate lung tumor suppressor locus."
      Yanaihara N., Kohno T., Takakura S., Takei K., Otsuka A., Sunaga N., Takahashi M., Yamazaki M., Tashiro H., Fukuzumi Y., Fujimori Y., Hagiwara K., Tanaka T., Yokota J.
      Genomics 72:169-179(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-80.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Trachea.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    7. Abts H.
      Thesis (1995), University of Cologne, Germany
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 421-584 (ISOFORM 1).
      Tissue: B-cell.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-33.
      Tissue: Platelet.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156; LYS-224; LYS-240; LYS-272 AND LYS-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases."
      Xu Y., Bhargava G., Wu H., Loeber G., Tong L.
      Structure 7:877-889(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    12. "Structure of a closed form of human malic enzyme and implications for catalytic mechanism."
      Yang Z., Floyd D.L., Loeber G., Tong L.
      Nat. Struct. Biol. 7:251-257(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-584 IN COMPLEX WITH NAD; DIVALENT METAL ION AND SUBSTRATE ANALOG, HOMOTETRAMERIZATION.
    13. "Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate."
      Yang Z., Lanks C.W., Tong L.
      Structure 10:951-960(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-573 IN COMPLEX WITH ATP; MANGANESE; ALLOSTERIC ACTIVATOR AND SUBSTRATE ANALOG, MUTAGENESIS OF ARG-67 AND ARG-91, HOMOTETRAMERIZATION.
    14. "Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism."
      Tao X., Yang Z., Tong L.
      Structure 11:1141-1150(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-584 IN COMPLEX WITH SUBSTRATE; NAD; MANGANESE AND ALLOSTERIC ACTIVATOR, ENZYME MECHANISM.

    Entry informationi

    Entry nameiMAOM_HUMAN
    AccessioniPrimary (citable) accession number: P23368
    Secondary accession number(s): B2R8J2
    , Q9BWL6, Q9BYG1, Q9H4B2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    This isoenzyme can also use NADP+ but is more effective with NAD+.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3