Any feedback?
Information on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase
for references in articles please use BRENDA:EC2.3.1.61Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.61 dihydrolipoyllysine-residue succinyltransferaseIUBMB Comments
A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
Specify your search results
Word Map
- 2.3.1.61
- pdc-e2
- autoantigens
-
bcoadc-e2
- kgdhc
-
antimitochondrial
-
autoepitopes
- medicine
-
bcoadc
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
dihydrolipoamide succinyltransferase, ogdc-e2, dihydrolipoyl succinyltransferase, dihydrolipoamide s-succinyltransferase, dihydrolipoyl transsuccinylase, lipoate succinyltransferase, dihydrolipoyllysine-residue succinyltransferase, lipoyl transsuccinylase, dihydrolipoyl succinyl transferase, e2 component of alpha-ketoglutarate dehydrogenase complex, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydrolipoamide S-succinyltransferase
dihydrolipoamide succinyltransferase
dihydrolipoic transsuccinylase
-
-
-
-
dihydrolipolyl transsuccinylase
-
-
-
-
dihydrolipoyl succinyltransferase
dihydrolipoyl transsuccinylase
-
-
-
-
DLST
E2 component of alpha-ketoglutarate dehydrogenase complex
KGD2
lipoate succinyltransferase
-
-
-
-
lipoic transsuccinylase
-
-
-
-
lipoyl transsuccinylase
-
-
-
-
SucB
succinyl-CoA:dihydrolipoate S-succinyltransferase
-
-
-
-
dihydrolipoamide succinyltransferase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
oxidative decarboxylation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase
A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9032-28-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
succinyl-CoA + dihydrolipoyllysine
CoA + succinyldihydrolipoyllysine
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
additional information
?
-
-
the DLST gene is bifunctionally involved in mitochondrial energy metabolism, the full-length DLST protein is involved in the Krebs cycle and the truncated version, MIRTD, contributes to the biogenesis of the respiratory chain. The genotype of the DLST gene is associated with Alztheimers disease without a change of amino acid residues in the DLST protein: through a decrease in the expression of the truncated gene product MIRTD and the function of MIRTD. It remains unclear how much MIRTD actually contributes to the pathogenesis of Alzheimers disease
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex
-
-
?
succinyl-CoA + DL-dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + DL-dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
r
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
Xanthomonas citri 29-1
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
additional information
?
-
-
the DLST gene is bifunctionally involved in mitochondrial energy metabolism, the full-length DLST protein is involved in the Krebs cycle and the truncated version, MIRTD, contributes to the biogenesis of the respiratory chain. The genotype of the DLST gene is associated with Alztheimers disease without a change of amino acid residues in the DLST protein: through a decrease in the expression of the truncated gene product MIRTD and the function of MIRTD. It remains unclear how much MIRTD actually contributes to the pathogenesis of Alzheimers disease
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
-
-
-
?
succinyl-CoA + dihydrolipoamide
CoA + S-succinyldihydrolipoamide
-
plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
r
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
Xanthomonas citri 29-1
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Lipoyl-protein
-
transsuccinylase core consists of 24 similar polypeptide chains, 12 of these chains contain a covalently bound lipoyl moiety
Lipoyl-protein
-
enzyme contains 8 mol of protein-bound lipoic acid per mol of enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2,4-dichloro-3-[[(prop-2-yn-1-yl)oxy]methyl]phenyl)-5-(ethanesulfonyl)-1,3,4-oxadiazole
-
-
2-(2,4-dichloro-3-[[(prop-2-yn-1-yl)oxy]methyl]phenyl)-5-(methanesulfonyl)-1,3,4-oxadiazole
-
-
2-(4-fluoro-3-[[(prop-2-yn-1-yl)oxy]methyl]phenyl)-5-(methanesulfonyl)-1,3,4-oxadiazole
-
-
2-(ethanesulfonyl)-5-(4-fluoro-3-[[(prop-2-yn-1-yl)oxy]methyl]phenyl)-1,3,4-oxadiazole
-
-
2-(ethanesulfonyl)-5-(4-[[(prop-2-yn-1-yl)oxy]methyl]phenyl)-1,3,4-oxadiazole
-
-
2-(methanesulfonyl)-5-(4-[[(prop-2-yn-1-yl)oxy]methyl]phenyl)-1,3,4-oxadiazole
-
-
2-(methylsulfonyl)-5-(4-fluoro-3-((prop-2-yn-1-yloxy)methyl)-phenyl)-1,3,4-oxadiazole
-
-
2-(methylsulfonyl)-5-(4-fluoro-3-((prop-2-yn-1-yloxy)methyl)-phenyl)-1,3,4-oxadiazole
-
-
coenzyme Q0
-
formation of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate complex (i.e. dihydrolipoamide succinyltransferase) partially explains the cellular toxicity of coenzyme Q0
coenzyme Q0
-
formation of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate complex (i.e. dihydrolipoamide succinyltransferase) partially explains the cellular toxicity of coenzyme Q0
additional information
-
no activity with 5-(4-fluoro-3-((prop-2-yn-1-yloxy)methyl)phenyl)-1,3,4-oxadiazol-2-ol
-
additional information
-
no activity with 5-(4-fluoro-3-((prop-2-yn-1-yloxy)methyl)phenyl)-1,3,4-oxadiazol-2-ol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
An unspliced cDNA for human dihydrolipoamide succinyltransferase: characterization and mapping of the gene to chromosome 14q24.2-q24.3.
Alzheimer Disease
Brain protein and alpha-ketoglutarate dehydrogenase complex activity in Alzheimer's disease.
Alzheimer Disease
Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: on defects in the cytochrome c oxidase complex and aldehyde detoxification.
Alzheimer Disease
Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex.
Alzheimer Disease
Mutation analysis of the chromosome 14q24.3 dihydrolipoyl succinyltransferase (DLST) gene in patients with early-onset Alzheimer disease.
Alzheimer Disease
Substantial linkage disequilibrium across the dihydrolipoyl succinyltransferase gene region without Alzheimer's disease association.
Autoimmune Diseases
Persistence of autoantibodies against recombinant mitochondrial and nuclear pore proteins after orthotopic liver transplantation for primary biliary cirrhosis.
Cardiomegaly
Inhibition of MicroRNA-146a and Overexpression of Its Target Dihydrolipoyl Succinyltransferase Protect Against Pressure Overload-Induced Cardiac Hypertrophy and Dysfunction.
Cat-Scratch Disease
The Bartonella henselae sucB gene encodes a dihydrolipoamide succinyltransferase protein reactive with sera from patients with cat-scratch disease.
dihydrolipoyllysine-residue succinyltransferase deficiency
Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition.
Graves Disease
Identification Of New Rare Variants Associated With Familial Autoimmune Thyroid Diseases By Deep Sequencing Of Linked Loci.
Liver Cirrhosis, Biliary
Definition of antigen specificity for antimitochondrial proteins detected by Western blotting using native mitochondrial proteins in primary biliary cirrhosis.
Liver Cirrhosis, Biliary
Development of an enzyme immune assay for detecting M2 autoantibodies specific for primary biliary cirrhosis.
Liver Cirrhosis, Biliary
Immunoreactivity of porcine heart dihydrolipoamide acetyl- and succinyl-transferases (PDC-E2, OGDC-E2) with primary biliary cirrhosis sera: characterization of the autoantigenic region and effects of enzymatic delipoylation and relipoylation.
Liver Cirrhosis, Biliary
In situ nucleic acid detection of PDC-E2, BCOADC-E2, OGDC-E2, PDC-E1alpha, BCOADC-E1alpha, OGDC-E1, and the E3 binding protein (protein X) in primary biliary cirrhosis.
Liver Cirrhosis, Biliary
Inhibition of alpha-ketoglutarate dehydrogenase activity by a distinct population of autoantibodies recognizing dihydrolipoamide succinyltransferase in primary biliary cirrhosis.
Liver Cirrhosis, Biliary
Persistence of autoantibodies against recombinant mitochondrial and nuclear pore proteins after orthotopic liver transplantation for primary biliary cirrhosis.
Liver Cirrhosis, Biliary
Promiscuous T cells selected by Escherichia coli: OGDC-E2 in primary biliary cirrhosis.
Memory Disorders
Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition.
Neoplasms
Dihydrolipoamide dehydrogenase regulates cystine deprivation-induced ferroptosis in head and neck cancer.
Neuroblastoma
Metabolic Enzyme DLST Promotes Tumor Aggression and Reveals a Vulnerability to OXPHOS Inhibition in High-Risk Neuroblastoma.
Spinocerebellar Ataxias
Immunoreactive levels of alpha-ketoglutarate dehydrogenase subunits in Friedreich's ataxia and spinocerebellar ataxia type 1.
Thyroiditis
Identification Of New Rare Variants Associated With Familial Autoimmune Thyroid Diseases By Deep Sequencing Of Linked Loci.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY