Malate dehydrogenase

Details

Name
Malate dehydrogenase
Synonyms
  • 1.1.1.37
Gene Name
mdh
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016007|Malate dehydrogenase
MKVAVLGAAGGIGQALALLLKTQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKIKGFSG
EDATPALEGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVQQVAKTCPKACIGIITNP
VNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPGEVEVPVIGGHSGV
TILPLLSQVPGVSFTEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQAAARFGLSLVR
ALQGEQGVVECAYVEGDGQYARFFSQPLLLGKNGVEERKSIGTLSAFEQNALEGMLDTLK
KDIALGEEFVNK
Number of residues
312
Molecular Weight
32337.065
Theoretical pI
5.46
GO Classification
Functions
L-malate dehydrogenase activity / malate dehydrogenase activity / oxidoreductase activity
Processes
anaerobic respiration / fermentation / glycolytic process / malate metabolic process / tricarboxylic acid cycle
Components
cytoplasm / cytosol / extrinsic component of membrane / membrane
General Function
Oxidoreductase activity
Specific Function
Catalyzes the reversible oxidation of malate to oxaloacetate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016008|Malate dehydrogenase (mdh)
ATGAAAGTCGCAGTCCTCGGCGCTGCTGGCGGTATTGGCCAGGCGCTTGCACTACTGTTA
AAAACCCAACTGCCTTCAGGTTCAGAACTCTCTCTGTATGATATCGCTCCAGTGACTCCC
GGTGTGGCTGTCGATCTGAGCCATATCCCTACTGCTGTGAAAATCAAAGGTTTTTCTGGT
GAAGATGCGACTCCGGCGCTGGAAGGCGCAGATGTCGTTCTTATCTCTGCAGGCGTAGCG
CGTAAACCGGGTATGGATCGTTCCGACCTGTTTAACGTTAACGCCGGCATCGTGAAAAAC
CTGGTACAGCAAGTTGCGAAAACCTGCCCGAAAGCGTGCATTGGTATTATCACTAACCCG
GTTAACACCACAGTTGCAATTGCTGCTGAAGTGCTGAAAAAAGCCGGTGTTTATGACAAA
AACAAACTGTTCGGCGTTACCACGCTGGATATCATTCGTTCCAACACCTTTGTTGCGGAA
CTGAAAGGCAAACAGCCAGGCGAAGTTGAAGTGCCGGTTATTGGCGGTCACTCTGGTGTT
ACCATTCTGCCGCTGCTGTCACAGGTTCCTGGCGTTAGTTTTACCGAGCAGGAAGTGGCT
GATCTGACCAAACGCATCCAGAACGCGGGTACTGAAGTGGTTGAAGCGAAGGCCGGTGGC
GGGTCTGCAACCCTGTCTATGGGCCAGGCAGCTGCACGTTTTGGTCTGTCTCTGGTTCGT
GCACTGCAGGGCGAACAAGGCGTTGTCGAATGTGCCTACGTTGAAGGCGACGGTCAGTAC
GCCCGTTTCTTCTCTCAACCGCTGCTGCTGGGTAAAAACGGCGTGGAAGAGCGTAAATCT
ATCGGTACCCTGAGCGCATTTGAACAGAACGCGCTGGAAGGTATGCTGGATACGCTGAAG
AAAGATATCGCCCTGGGCGAAGAGTTCGTTAATAAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP61889
UniProtKB Entry NameMDH_ECOLI
GenBank Protein ID41989
GenBank Gene IDY00129
General References
  1. McAlister-Henn L, Blaber M, Bradshaw RA, Nisco SJ: Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase. Nucleic Acids Res. 1987 Jun 25;15(12):4993. [Article]
  2. Vogel RF, Entian KD, Mecke D: Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase. Arch Microbiol. 1987;149(1):36-42. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Sutherland P, McAlister-Henn L: Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase. J Bacteriol. 1985 Sep;163(3):1074-9. [Article]
  6. Fernley RT, Lentz SR, Bradshaw RA: Malate dehydrogenase: isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms. Biosci Rep. 1981 Jun;1(6):497-507. [Article]
  7. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  8. Charnock C: Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure. J Bacteriol. 1997 Jun;179(12):4066-70. [Article]
  9. Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C: Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5011-5. [Article]
  10. Nystrom T, Larsson C, Gustafsson L: Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. EMBO J. 1996 Jul 1;15(13):3219-28. [Article]
  11. Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608. [Article]
  12. Boyd EF, Nelson K, Wang FS, Whittam TS, Selander RK: Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1280-4. [Article]
  13. Pupo GM, Karaolis DK, Lan R, Reeves PR: Evolutionary relationships among pathogenic and nonpathogenic Escherichia coli strains inferred from multilocus enzyme electrophoresis and mdh sequence studies. Infect Immun. 1997 Jul;65(7):2685-92. [Article]
  14. Pupo GM, Lan R, Reeves PR, Baverstock PR: Population genetics of Escherichia coli in a natural population of native Australian rats. Environ Microbiol. 2000 Dec;2(6):594-610. [Article]
  15. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  16. Hall MD, Levitt DG, Banaszak LJ: Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution. J Mol Biol. 1992 Aug 5;226(3):867-82. [Article]
  17. Hall MD, Banaszak LJ: Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution. J Mol Biol. 1993 Jul 5;232(1):213-22. [Article]
  18. Bell JK, Yennawar HP, Wright SK, Thompson JR, Viola RE, Banaszak LJ: Structural analyses of a malate dehydrogenase with a variable active site. J Biol Chem. 2001 Aug 17;276(33):31156-62. Epub 2001 Jun 1. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails