F1C7I4 · MDHC_TAESO
- ProteinMalate dehydrogenase, cytoplasmic
- GeneMDH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids332 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Malate dehydrogenase. Has no activity with NADPH as substrate. Does not show lactate dehydrogenase activity.
Catalytic activity
- (S)-malate + NAD+ = H+ + NADH + oxaloacetate
Activity regulation
By arsenate for both the forward and reverse reactions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
100 μM | L-malate | 9.6 | ||||
42 μM | NAD | 9.6 | ||||
44 μM | oxaloacetate | 8 | ||||
167 μM | NADH | 8 | ||||
215 μM | L-malate | 9.6 | ||||
50 μM | NAD | 9.6 | ||||
2.4 μM | oxaloacetate | 7.6 | ||||
48 μM | NADH | 7.6 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
77.03 μmol/min/mg | 9.6 | toward L-malate | |||
79.12 μmol/min/mg | 9.6 | toward NAD | |||
450.3 μmol/min/mg | 8 | toward oxaloacetate | |||
721.4 μmol/min/mg | 8 | toward NADH | |||
87.8 μmol/min/mg | 9.6 | toward L-malate | |||
104 μmol/min/mg | 9.6 | toward NAD | |||
1490 μmol/min/mg | 7.6 | toward oxaloacetate | |||
1714 μmol/min/mg | 7.6 | toward NADH |
kcat is 47.4 sec-1 for L-malate. kcat is 385.6 sec-1 for NAD. kcat is 665.34 sec-1 for oxaloacetate. kcat is 962.66 sec-1 for NADH.
pH Dependence
Optimum pH is 7.6 for oxaloacetate reduction and 9.6 for malate oxidation (PubMed:19277715, PubMed:21439955).
Stable between pH 6.8-8.5 for the forward reaction (PubMed:19277715).
Stable between pH 6.8-8.5 for the forward reaction (PubMed:19277715).
Temperature Dependence
Has highest activity between 5-40 degrees Celsius. No activity at 60 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11-17 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAAGQIA | ||||||
Binding site | 42 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | substrate | ||||
Sequence: R | ||||||
Binding site | 98 | substrate | ||||
Sequence: R | ||||||
Binding site | 105 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 112 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 129-131 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VGN | ||||||
Binding site | 131 | substrate | ||||
Sequence: N | ||||||
Binding site | 162 | substrate | ||||
Sequence: R | ||||||
Active site | 187 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | L-malate dehydrogenase activity | |
Molecular Function | NAD binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | malate metabolic process | |
Biological Process | NADH metabolic process | |
Biological Process | oxaloacetate metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMalate dehydrogenase, cytoplasmic
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Cestoda > Eucestoda > Cyclophyllidea > Taeniidae > Taenia
Accessions
- Primary accessionF1C7I4
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000438645 | 2-332 | Malate dehydrogenase, cytoplasmic | |||
Sequence: PGPLRVLITGAAGQIAYNLSNMVANGNLFGKDQKIILHLLDIPEAKTVLEGVVMELQDCAFTVLEGIVPTHCLKEAFTDIDVALMVGAMPRKQGMERRDLLSSNVKIFKDQGEALEKYAKKTVKVLVVGNPANTNCLIMSKYAPSIPKENFTALSRLDHNRAIYQVAAKVGVPSECVKNVCIWGNHSNKQFPDLAHAVVTKGGKQHPAKELINDEKWVKEVFTPCVQNRGAAVIGLRKLSSAASAAKAIVDQMHDWWFGTKEGEWVSMSVYSTGEHYGAPKDIYFSFPVTIKNGHYKVVDGLAMDEWGKGLFKITADELVDEREVALSSFK |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length332
- Mass (Da)36,517
- Last updated2011-05-03 v1
- Checksum83B104F5E1A7A3F1
Keywords
- Technical term