Identification
NameMalate dehydrogenase, cytoplasmic
SynonymsNot Available
Gene NameMDH2
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific FunctionThe isoenzyme MDH2 may function primarily in the glyoxylate cycle
Cellular LocationCytoplasm
SMPDB Pathways
Aspartate metabolismPW002375 ThumbThumb?image type=greyscaleThumb?image type=simple
Glyoxylate cyclePW002419 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
TCA CyclePW002377 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Citrate cycle (TCA cycle)ec00020 Map00020
Glyoxylate and dicarboxylate metabolismec00630 Map00630
Methane metabolismec00680 Map00680
Pyruvate metabolismec00620 Map00620
SMPDB Reactions
NADH + hydron + Oxalacetic acid(S)-Malic acid + NAD
(S)-Malic acid + NADhydron + NADH + Oxalacetic acid
KEGG Reactions
NAD + (S)-malate(2-)NADH + hydron + Oxalacetic acid
Metabolites
YMDB IDNameView
YMDB00110NADShow
YMDB00143NADHShow
YMDB00235Oxalacetic acidShow
YMDB00280(S)-Malic acidShow
YMDB00412NAD(+)Show
YMDB00862hydronShow
GO Classification
Component
Not Available
Function
catalytic activity
L-malate dehydrogenase activity
malate dehydrogenase activity
binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
carboxylic acid metabolic process
cellular carbohydrate metabolic process
dicarboxylic acid metabolic process
metabolic process
malate metabolic process
cellular metabolic process
primary metabolic process
carbohydrate metabolic process
oxidation reduction
organic acid metabolic process
oxoacid metabolic process
Gene Properties
Chromosome Locationchromosome 15
LocusYOL126C
Gene Sequence>1134 bp ATGCCTCACTCAGTTACACCATCCATAGAACAAGATTCGTTAAAAATTGCCATTTTAGGT GCTGCCGGTGGTATCGGGCAGTCGTTATCGCTGCTTTTGAAAGCTCAGTTGCAATACCAG TTAAAGGAGAGCAACCGGAGCGTTACCCACATTCATCTGGCTCTTTACGATGTCAACCAA GAAGCCATCAACGGTGTTACCGCCGACTTGTCTCATATAGACACCCCCATTTCCGTGTCG AGCCACTCTCCTGCAGGTGGCATTGAGAACTGTTTGCATAACGCTTCTATTGTTGTCATT CCTGCAGGTGTTCCAAGAAAACCTGGCATGACTCGTGATGACTTATTTAACGTGAATGCT GGTATCATTAGCCAGCTCGGTGATTCTATTGCAGAATGTTGTGATCTTTCCAAGGTCTTC GTTCTTGTCATTTCCAACCCTGTTAATTCTTTAGTCCCAGTGATGGTTTCTAACATTCTT AAGAACCATCCTCAGTCTAGAAATTCCGGCATTGAAAGAAGGATCATGGGTGTCACCAAG CTCGACATTGTCAGAGCGTCCACTTTTCTACGTGAGATAAACATTGAGTCAGGGCTAACT CCTCGTGTTAACTCCATGCCTGACGTCCCTGTAATTGGCGGGCATTCTGGCGAGACTATT ATTCCGTTGTTTTCACAGTCAAACTTCCTATCGAGATTAAATGAGGATCAATTGAAATAT TTAATACATAGAGTCCAATACGGTGGTGATGAAGTGGTCAAGGCCAAGAACGGTAAAGGT AGTGCTACCTTATCGATGGCCCATGCCGGTTATAAGTGTGTTGTCCAATTTGTTTCTTTG TTATTGGGTAACATTGAGCAGATCCATGGAACCTACTATGTGCCATTAAAAGATGCGAAC AACTTCCCCATTGCTCCTGGGGCAGATCAATTATTGCCTCTGGTGGACGGTGCAGACTAC TTTGCCATACCATTAACTATTACTACAAAGGGTGTTTCCTATGTGGATTATGACATCGTT AATAGGATGAACGACATGGAACGCAACCAAATGTTGCCAATTTGCGTCTCCCAGTTAAAG AAAAATATCGATAAGGGCTTGGAATTCGTTGCATCGAGATCTGCATCATCTTAA
Protein Properties
Pfam Domain Function
Protein Residues377
Protein Molecular Weight40730.39844
Protein Theoretical pI6.9
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Malate dehydrogenase, cytoplasmic MPHSVTPSIEQDSLKIAILGAAGGIGQSLSLLLKAQLQYQLKESNRSVTHIHLALYDVNQ EAINGVTADLSHIDTPISVSSHSPAGGIENCLHNASIVVIPAGVPRKPGMTRDDLFNVNA GIISQLGDSIAECCDLSKVFVLVISNPVNSLVPVMVSNILKNHPQSRNSGIERRIMGVTK LDIVRASTFLREINIESGLTPRVNSMPDVPVIGGHSGETIIPLFSQSNFLSRLNEDQLKY LIHRVQYGGDEVVKAKNGKGSATLSMAHAGYKCVVQFVSLLLGNIEQIHGTYYVPLKDAN NFPIAPGADQLLPLVDGADYFAIPLTITTKGVSYVDYDIVNRMNDMERNQMLPICVSQLK KNIDKGLEFVASRSASS
References
External Links
ResourceLink
Saccharomyces Genome Database MDH2
Uniprot IDP22133
Uniprot NameMDHC_YEAST
GenBank Gene IDM62808
Genebank Protein ID171916
General Reference
  • Minard, K. I., McAlister-Henn, L. (1991). "Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene from Saccharomyces cerevisiae: evidence for three isozymes of yeast malate dehydrogenase." Mol Cell Biol 11:370-380.1986231
  • Casamayor, A., Khalid, H., Balcells, L., Aldea, M., Casas, C., Herrero, E., Arino, J. (1996). "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase, the ribosomal L25 gene and four new open reading frames." Yeast 12:1013-1020.8896265
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • Kopetzki, E., Entian, K. D., Lottspeich, F., Mecke, D. (1987). "Purification procedure and N-terminal amino acid sequence of yeast malate dehydrogenase isoenzymes." Biochim Biophys Acta 912:398-403.3552052
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956