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Information on EC 1.1.1.27 - L-lactate dehydrogenase and Organism(s) Sus scrofa
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1.1.1.27 L-lactate dehydrogenaseIUBMB Comments
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lactate dehydrogenase, lactic dehydrogenase, ldh-a, lactate dehydrogenase a, l-lactate dehydrogenase, ldh-5, lactic acid dehydrogenase, ldh-1, pfldh, alpha-hydroxybutyrate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, lactate
-
-
-
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
-
-
-
-
Immunogenic protein p36
-
-
-
-
L(+)-nLDH
-
-
-
-
L-(+)-lactate dehydrogenase
-
-
-
-
L-lactic acid dehydrogenase
-
-
-
-
L-lactic dehydrogenase
-
-
-
-
L-LDH
-
-
-
-
lactate dehydrogenase
lactate dehydrogenase NAD-dependent
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic dehydrogenase
-
-
-
-
LDH
NAD-lactate dehydrogenase
-
-
-
-
proteins, specific or class, anoxic stress response, p34
-
-
-
-
lactate dehydrogenase
-
-
-
-
LDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
CAS REGISTRY NUMBER
COMMENTARY
9001-60-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lactate + NAD+
pyruvate + NADH + H+
-
an encounter complex is formed between LDH-NAD+ and lactate, collapses to form a chemically active species and loop closure/opening steps
-
-
?
oxamate + NADH
?
-
two distinct active site LDH/NADH-oxamate complex conformations, a major populated structure wherein all significant hydrogen-bonding patterns are formed at the active site between protein and bound ligand necessary for the catalytically productive Michaelis complex and, a minor structure in a configuration of the active site that is unfavorable to carry out catalyzed chemistry. This latter structure likely simulates a dead-end complex in the reaction mixture. The evolution of the encounter complex between LDH/NADH and oxamate collapses via a branched reaction pathway to form the major and minor bound species. Once the encounter complex is formed between LDH/NADH and substrate, the ternary protein-ligand complex appears to fold to form a compact productive complex in an all or nothing like fashion with all the important molecular interactions coming together at the same time
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
-
an encounter complex is formed between LDH-NADH and pyruvate, collapses to form a chemically active species and loop closure/opening steps
-
-
?
additional information
?
-
-
the heart-type isozyme interacts with liposomes made of acidic phospholipids, such as phosphatidylserine or cardiolipin, most effectively at low pH close to the isoelectric point of the isozyme of pH 5.5 strongly involving the enzyme's NADH-cofactor binding site, no interaction with liposomes of the muscle-type isozyme, overview
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + NADH + H+
(S)-lactate + NAD+
-
D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
the NADH-cofactor binding site of heart LDH is involved in the interaction of the isozyme with liposomes made of acidic phospholipids, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cardiolipin
-
IC50: 0.00005 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
o-phthalaldehyde
-
modification not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding
phosphatidylserine
-
IC50: 0.0013 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
additional information
-
NADH, NAD+, ATP, ADP, AMP, and pyruvate inhibit the interaction of the heart-type isozyme with acidic phospholipid liposomes, potency in descending order. NADP+, GTP, CTP, UTP and lactate are ineffective, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
stopped-flow kinetics, steady-state kinetics, and thermodynamics of free and NADH-bound enzyme, overview
-
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
-
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
pyruvate
-
the enzyme shows hyperbolic dependence on the substrate concentration
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
pyruvate
-
the enzyme shows hyperbolic dependence on the substrate concentration
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00005
cardiolipin
Sus scrofa
-
IC50: 0.00005 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
0.0013
phosphatidylserine
Sus scrofa
-
IC50: 0.0013 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme shows hyperbolic dependence on the substrate concentration
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
contains a skeletal muscle type and heart type mixed heterotetrameric enzyme, H2M2
additional information
contains a skeletal muscle type homotetrameric enzyme, M4
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
additional information
-
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
lactate dehydrogenase (LDH) is a glycolytic enzyme that catalyzes the final step of glycolysis and produces NAD+
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LDHB_PIG
334
0
36612
Swiss-Prot
other Location (Reliability: 2)
LDHA_PIG
332
0
36619
Swiss-Prot
other Location (Reliability: 2)
LDHC_PIG
332
0
36053
Swiss-Prot
other Location (Reliability: 2)
A0A8D0SRQ5_PIG
332
0
36720
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D0SYC1_PIG
377
0
41398
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D0XUU2_PIG
332
0
36025
TrEMBL
other Location (Reliability: 2)
A0A8D0PXP6_PIG
332
0
36053
TrEMBL
other Location (Reliability: 2)
A0A5G2QUB8_PIG
183
0
19735
TrEMBL
other Location (Reliability: 2)
A0A8D0PX14_PIG
225
0
24504
TrEMBL
other Location (Reliability: 2)
A0A0K0KW08_PIG
381
0
41861
TrEMBL
Mitochondrion (Reliability: 1)
D2SW96_PIG
332
0
36591
TrEMBL
other Location (Reliability: 2)
A0A4X1T9Q1_PIG
388
0
42739
TrEMBL
other Location (Reliability: 4)
A0A8D0PWV6_PIG
442
0
48025
TrEMBL
other Location (Reliability: 3)
A0A8D0SNN0_PIG
345
0
37818
TrEMBL
other Location (Reliability: 3)
A0A286ZNX3_PIG
417
0
46039
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D1QY15_PIG
232
0
25023
TrEMBL
other Location (Reliability: 2)
A0A4X1T7P1_PIG
241
0
26037
TrEMBL
other Location (Reliability: 2)
A0A8D1Z793_PIG
334
0
36536
TrEMBL
other Location (Reliability: 2)
A0A4X1VNU5_PIG
334
0
36622
TrEMBL
other Location (Reliability: 2)
A0A4X1VED5_PIG
377
0
41416
TrEMBL
Mitochondrion (Reliability: 1)
A7E1T1_PIG
199
0
21683
TrEMBL
other Location (Reliability: 2)
A0A4X1T6G7_PIG
417
0
46069
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D0PY76_PIG
241
0
26038
TrEMBL
other Location (Reliability: 2)
A0A4X1T837_PIG
361
0
39754
TrEMBL
other Location (Reliability: 4)
A0A5G2QHL7_PIG
334
0
36622
TrEMBL
other Location (Reliability: 2)
A0A4X1T9D9_PIG
332
0
36052
TrEMBL
other Location (Reliability: 2)
A0A4X1VAI4_PIG
389
0
42843
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8D0IST4_PIG
388
0
42894
TrEMBL
other Location (Reliability: 4)
A0A8D1QB28_PIG
417
0
46039
TrEMBL
Mitochondrion (Reliability: 5)
A0A5G2QLD7_PIG
241
0
26038
TrEMBL
other Location (Reliability: 2)
F1SFX0_PIG
332
0
36053
TrEMBL
other Location (Reliability: 2)
A0A4X1T6H3_PIG
442
0
47957
TrEMBL
other Location (Reliability: 5)
A0A4X1T7S9_PIG
183
0
19734
TrEMBL
other Location (Reliability: 2)
A0A8D0IMU6_PIG
403
0
43781
TrEMBL
other Location (Reliability: 5)
A0A286ZXT7_PIG
443
0
48028
TrEMBL
other Location (Reliability: 5)
A0A8D0XEC1_PIG
389
0
42827
TrEMBL
other Location (Reliability: 5)
A0A480X8T8_PIG
374
0
41157
TrEMBL
Mitochondrion (Reliability: 4)
D4N875_PIG
155
0
17079
TrEMBL
other Location (Reliability: 2)
A0A8D0YZV9_PIG
332
0
36738
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D2BTM1_PIG
389
0
42785
TrEMBL
other Location (Reliability: 5)
A0A8D0PXZ1_PIG
183
0
19735
TrEMBL
other Location (Reliability: 2)
A0A8D1IY58_PIG
377
0
41398
TrEMBL
Mitochondrion (Reliability: 1)
A0A4X1T888_PIG
225
0
24504
TrEMBL
other Location (Reliability: 2)
A0A8D0ISQ8_PIG
402
0
44382
TrEMBL
Mitochondrion (Reliability: 4)
A0A5G2QSJ4_PIG
225
0
24504
TrEMBL
other Location (Reliability: 2)
A0A5S6GD60_PIG
388
0
42739
TrEMBL
other Location (Reliability: 4)
A0A287AFC1_PIG
345
0
37818
TrEMBL
other Location (Reliability: 3)
A0A385JGP0_PIG
332
0
36619
TrEMBL
other Location (Reliability: 2)
A0A287B2H7_PIG
361
0
39754
TrEMBL
other Location (Reliability: 4)
A0A8D1WTH6_PIG
377
0
41374
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D0IL65_PIG
346
0
37963
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
the heterotetrameric LDH (H2M2) from swine brain is formed by two subunit of LDHA and two subunits of LDHB
additional information
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
-
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
modification by o-phthalaldehyde not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zheng, Y.B.; Wang, Z.; Chen, B.Y.; Wang, X.C.
Multiple effects of chemical reagent on enzyme: o-phthalaldehyde-induced inactivation, dissociation and partial unfolding of lactate dehydrogenase from pig heart
Int. J. Biol. Macromol.
32
191-197
2003
Sus scrofa
Terlecki, G.; Czapinska, E.; Rogozik, K.; Lisowski, M.; Gutowicz, J.
Investigation of the interaction of pig muscle lactate dehydrogenase with acidic phospholipids at low pH
Biochim. Biophys. Acta
1758
133-144
2006
Sus scrofa
Svedruzic, Z.M.; Spivey, H.O.
Interaction between mammalian glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase from heart and muscle
Proteins
63
501-511
2006
Sus scrofa
Qiu, L.; Gulotta, M.; Callender, R.
Lactate dehydrogenase undergoes a substantial structural change to bind its substrate
Biophys. J.
93
1677-1686
2007
Sus scrofa
Terlecki, G.; Czapi?ska, E.; Hotowy, K.
Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme
Cell. Mol. Biol. Lett.
12
378-395
2007
Sus scrofa
Zhadin, N.; Gulotta, M.; Callender, R.
Probing the role of dynamics in hydride transfer catalyzed by lactate dehydrogenase
Biophys. J.
95
1974-1984
2008
Sus scrofa
Deng, H.; Brewer, S.; Vu, D.M.; Clinch, K.; Callender, R.; Dyer, R.B.
On the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase
Biophys. J.
95
804-813
2008
Sus scrofa
Goto, T.; Sugawara, K.; Nakamura, S.; Kidokoro, S.I.; Wakui, H.; Nunomura, W.
Enzymatic and thermodynamic profiles of a heterotetramer lactate dehydrogenase isozyme in swine
Biochem. Biophys. Res. Commun.
479
860-867
2016
Sus scrofa (P00336), Sus scrofa (P00339), Sus scrofa
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