|Gene:||ldh||Accession Number: G-6661 (MetaCyc)|
Species: Lactobacillus casei
Subunit composition of
L-lactate dehydrogenase = [Ldh]4
L-lactate dehydrogenase subunit = Ldh
Despite the strikingly different enzymatic characteristics of the allosteric L-lactate dehydrogenase of Lactobacillus casei and of the non-allosteric vertebrate enzymes, they share a distinct homology (average identity: 37%). An especially high sequence homology can be identified within the active center (average identity: 70%) [Kim91a].
This enzyme has an acidic pH optimum of 5.5. Above this pH the affinity of the enzyme towards its activator, fructose 1,6-bisphosphate, is significantly reduced. This narrow pH tolerance is increases substantially in the presence of divalent metal ions, including Mn2+, Co2+, Cu2+, Cd2+, Ni2+, Fe2+ and Zn2+, but not Mg2+ [Hensel83].
Molecular Weight of Polypeptide: 35.399 kD (from nucleotide sequence), 34 kD (experimental) [Gordon76 ]
Molecular Weight of Multimer: 132 kD (experimental) [Gordon76]
Relationship Links: Entrez-Nucleotide:PART-OF:M76708 , InterPro:IN-FAMILY:IPR001236 , InterPro:IN-FAMILY:IPR001557 , InterPro:IN-FAMILY:IPR011304 , InterPro:IN-FAMILY:IPR015955 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR018177 , InterPro:IN-FAMILY:IPR022383 , Panther:IN-FAMILY:PTHR11540 , PDB:Structure:1LLC , PDB:Structure:2ZQY , PDB:Structure:2ZQZ , PDB:Structure:3VKU , PDB:Structure:3VKV , PDB:Structure:3VPF , Pfam:IN-FAMILY:PF00056 , Pfam:IN-FAMILY:PF02866 , Prints:IN-FAMILY:PR00086 , Prosite:IN-FAMILY:PS00064
|MultiFun Terms:||metabolism → energy metabolism, carbon → glycolysis|
Enzymatic reaction of: L-lactate dehydrogenase
EC Number: 220.127.116.11
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
This reaction is reversible.
Cofactors or Prosthetic Groups: NAD+
pH(opt): 5.5 [Holland75]
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493