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1.1.1.27: L-lactate dehydrogenase

This is an abbreviated version!
For detailed information about L-lactate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.27

Reaction

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

Synonyms

A4-LDH, AdhE, alpha-HBDH, alpha-hydroxybutyrate dehydrogenase, anaerobic lactate dehydrogenase, BbLDH, dehydrogenase, lactate, eLDHA, eLDHB, Epsilon crystallin, epsilon-crystallin, H4-L-lactate dehydrogenase, HBDH, heart LDH, Immunogenic protein p36, L(+)-nLDH, L-(+)-lactate dehydrogenase, L-lactate dehydrogenase, L-lactate dehydrogenase B, L-lactic acid dehydrogenase, L-lactic dehydrogenase, L-LDH, L-Ldh0845, L-nLDH, lactate dehydrogenase, lactate dehydrogenase 5, lactate dehydrogenase A, lactate dehydrogenase B, lactate dehydrogenase NAD-dependent, lactic acid dehydrogenase, lactic dehydrogenase, LctD, LDH, LDH-1, LDH-2, LDH-3, LDH-4, LDH-5, LDH-A, LDH-A4, LDH-m4, LDH1, LDH2, LdhA, LDHB, ldhL, LDHL1, LDHL2, LOX, LutACB, mL-LDH, mLDH, More, muscle LDH, NAD-dependent lactate dehydrogenase, NAD-lactate dehydrogenase, NGO0904, NGO0905, NGO0906, nitric oxideinducible l-lactate dehydrogenase, PfLDH, proteins, specific or class, anoxic stress response, p34, Sa-LDH-1, SMU.1115, SMU_1115, TeLdhL, Tsac_0416

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.27 L-lactate dehydrogenase

General Stability

General Stability on EC 1.1.1.27 - L-lactate dehydrogenase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of cofactor stabilizes all allozymes to urea inactivation
-
fructose-1,6-diphosphate is necessary to stabilize the tetrameric enzyme form
-
inactivation by pronase, trypsin and chymotrypsin
-
irreversible loss of activity after several hours when the concentration is below 0.1 mg protein per ml
-
Mn2+ and fructose 1,6-diphosphate are required during dialysis at pH 5.5, very unstable during dialysis at pH 7.5 although Mn2+ and fructose 1,6-diphosphate are added
-
modification by o-phthalaldehyde not only results in inactivation of the enzyme, but also leads to the enzyme‘s dissociation and partial unfolding
-
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH
-
NADH and fructose 1,6-diphosphate partially stabilize the 140000 Da molecular weight form against dissociation in triethanolamine-hydrochloride buffer at pH 8.0
-
PEG and trehalose stabilize the enzyme
-
stable to dilution in the range 0.2-0.01 mg protein per ml
-
the transition midpoints, 50% activity after 1 h incubation in guanidine HCl, are 0.77 M for the mutant enzyme with a deletion of 10 N-terminal amino acids, 0.92 M for the mutant with a deletion of 5 N-terminal amino acids and 1.7 M for the wild-type enzyme
-
very stable during 70 h dialysis in acetate buffer pH 5.5, in imidazol buffer, pH 6.5, in phosphate buffer pH 6.5 with dithioerythritol and in Tris-HCl buffer pH 7.5 with Mn2+ and fructose 1,6-diphosphate
-