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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: L-lactate dehydrogenase

Gene: ldh Accession Number: G-6661 (MetaCyc)

Species: Lactobacillus casei

Subunit composition of L-lactate dehydrogenase = [Ldh]4
         L-lactate dehydrogenase subunit = Ldh

Summary:
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%) [Kim91].

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]

Unification Links: ModBase:P00343 , Protein Model Portal:P00343 , SMR:P00343 , Swiss-Model:P00343 , UniProt:P00343

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

Gene-Reaction Schematic: ?

MultiFun Terms: metabolism energy metabolism, carbon glycolysis


Enzymatic reaction of: L-lactate dehydrogenase

EC Number: 1.1.1.27

(S)-lactate + NAD+ <=> pyruvate + NADH + H+

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.

In Pathways: homolactic fermentation , heterolactic fermentation , pyruvate fermentation to lactate

Cofactors or Prosthetic Groups: NAD+

Activators (Allosteric): fructose 1,6-bisphosphate [Hensel83]

Inhibitors (Unknown Mechanism): ADP [Gordon76] , ATP [Gordon76] , dihydroxyacetone phosphate [Gordon76] , D-gluconate 6-phosphate [Gordon76]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADH
10.0
[Gordon76]
pyruvate
1000.0
[Gordon76]

pH(opt): 5.5 [Holland75]


References

Gordon76: Gordon GL, Doelle HW (1976). "Purification, properties and immunological relationship of L (+)-lactate dehydrogenase from Lactobacillus casei." Eur J Biochem 67(2);543-55. PMID: 823016

Hensel83: Hensel R, Mayr U, Yang CY (1983). "The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei." Eur J Biochem 134(3);503-11. PMID: 6411465

Holland75: Holland R, Pritchard GG (1975). "Regulation of the L-lactase dehydrogenase from Lactobacillus casei by fructose-1,6-diphosphate and metal ions." J Bacteriol 121(3);777-84. PMID: 234946

Kim91: Kim SF, Baek SJ, Pack MY (1991). "Cloning and nucleotide sequence of the Lactobacillus casei lactate dehydrogenase gene." Appl Environ Microbiol 57(8);2413-7. PMID: 1768113


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc11.