Information on EC 3.2.2.6 - ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.2.6
-
RECOMMENDED NAME
GeneOntology No.
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclic ADP-ribose + H2O = ADP-D-ribose
show the reaction diagram
(1b)
-
-
-
NAD+ + H2O = ADP-D-ribose + nicotinamide
show the reaction diagram
NAD+ = cyclic ADP-ribose + nicotinamide
show the reaction diagram
(1a)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Nicotinate and nicotinamide metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+ glycohydrolase (cyclic ADP-ribose-forming)
This multiunctional enzyme catalyses both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes. In addition, the enzyme also catalyses EC 2.4.99.20, 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase. cf. EC 3.2.2.5, NAD+ glycohydrolase.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-46-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene cd38
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the CD38-cADPR signaling system is conserved during vertebrate evolution, phylogenetic tree
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,N6-etheno NAD+ + H2O
epsilon-ADP-ribose + nicotinamide + H+
show the reaction diagram
-
-
-
-
?
3-acetylpyridine + adenosine diphosphoribose
3-acetylpyridine adenine dinucleotide + phosphate
show the reaction diagram
-
transglycosylation activity, very poor hydrolytic activity with this substrate
-
-
?
3-acetylpyridine adenine dinucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
3-acetylpyridine hypoxanthine dinucleotide + H2O
?
show the reaction diagram
-
low activity
-
-
?
3-pyridine adenine dinucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
3-pyridinealdehyde hypoxanthine dinucleotide + H2O
?
show the reaction diagram
alpha-NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
beta-NAD+ + H2O
?
show the reaction diagram
cyclic ADP-ribose + H2O
?
show the reaction diagram
-
-
-
-
?
cyclic ADP-ribose + H2O
adenosine diphosphoribose + ?
show the reaction diagram
-
i.e. ADPR activity
-
-
?
cyclic ADP-ribose + H2O
ADP-D-ribose
show the reaction diagram
cyclic ADP-ribose + H2O
ADP-ribose
show the reaction diagram
-
-
-
-
?
epsilon-NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
epsilon-NADP+ + H2O
?
show the reaction diagram
-
-
-
-
?
NAD+
cyclic ADP-ribose + nicotinamide
show the reaction diagram
NAD+ + ?
cyclic ADP-ribose + ?
show the reaction diagram
-
i.e. cADPR activity
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
show the reaction diagram
NAD+ + H2O
ADP-ribose + nicotinamide
show the reaction diagram
-
-
-
-
?
NAD+ + H2O
cyclic ADP-ribose + nicotinamide + H+
show the reaction diagram
-
the cyclization and hydrolysis of NAD(P)+ occur optimally at physiological pH
-
-
?
NADP+ + H2O
ADP-ribose-P + nicotinamide
show the reaction diagram
-
80% activity compared to the activity with NAD+
-
-
?
NADP+ + H2O
nicotinamide + ADPribose-phosphate
show the reaction diagram
NADP+ + nicotinic acid
nicotinic acid adenine dinucleotide phosphate
show the reaction diagram
-
this reaction occurs only in acidic pH
-
-
?
NGD+ + H2O
cyclic GDP-ribose
show the reaction diagram
-
-
-
-
?
NGD+ + H2O
GDP-ribose + nicotinamide
show the reaction diagram
-
as effective as substrate as NAD+
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + H2O
?
show the reaction diagram
-
i.e. epsilonNAD+, used for a fluorometric assay
-
-
?
nicotinamide guanine dinucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
nicotinamide-hypoxanthine dinucleotide + H2O
?
show the reaction diagram
nicotinamide-hypoxanthine dinucleotide phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
thio-NAD+ + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cyclic ADP-ribose + H2O
ADP-D-ribose
show the reaction diagram
NAD+
cyclic ADP-ribose + nicotinamide
show the reaction diagram
NAD+ + H2O
ADP-D-ribose + nicotinamide
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase; at 2 mM 50% inhibition of NADase activity and 300% activation of ADPR activity
Cu2+
-
stimulation of cADPR activity
additional information
-
no effects by K+, Cd2+, Fe2+, Fe3+, and Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,N6-etheno NAD+
-
-
1-[2-azido-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]-3-carbamoylpyridinium
1-[5-O-[(benzyloxy)(hydroxy)phosphoryl]-2-deoxy-2-fluoro-L-erythro-pentofuranosyl]-3-carbamoylpyridinium
1-[5-O-[butoxy(hydroxy)phosphoryl]-2-deoxy-2-fluoro-D-threo-pentofuranosyl]-3-carbamoylpyridinium
2'-deoxy-2'-beta-D-fluoroarabinofuranoside NAD+
-
-
2'-deoxy-2'-beta-D-fluororibofuranoside NAD+
-
non-covalent complex of the inhibitor formed with enzyme mutant E218Q, PDB ID: 3ghh, and with wild-type enzyme, PDB ID: 3kou
3-aminopyridine
-
-
3-carbamoyl-1-[2-chloro-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-phosphono-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-phosphono-L-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-thiophosphono-L-erythro-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-[(hexyloxy)(hydroxy)phosphoryl]-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-[hydroxy(2-phenylethoxy)phosphoryl]-L-erythro-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-5-O-(diethoxyphosphoryl)-2-fluoro-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-5-O-[(ethenyloxy)(propoxy)phosphoryl]-2-fluoro-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[3-deoxy-3-fluoro-5-O-phosphono-L-threo-pentofuranosyl]pyridinium
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)chromenium
-
-
ADP-ribose
-
-
Ag+
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase; at 2 mM 50% inhibition of NADase activity and 300% activation of cADPR activity
arabinosyl 2'-fluoro-2'-deoxy-NAD
-
suicide substrate that inhibits CD38 ectoenzyme activity
arabinosyl-2'-fluoro-2'-deoxynicotinamide mononucleotide
Cr3+
-
; inhibition of NADase and adenosine diphosphate cyclase
cyanidin
-
-
delphinidin
-
-
fisetinidin
-
-
HClO4
-
5%, 2C, 10 min, 60% loss of the original activity
Isonicotinic acid hydrazide
-
-
kuromanin
-
-
luteolin
-
-
luteolinidin
-
-
malvidin
-
-
myricetin
-
-
nicotinamide
-
inhibition involves enzyme residue Trp181
Pb2+
-
complete inhibition at 2 mM; inhibition of NADase and adenosine diphosphate cyclase
pelargonidin
-
-
peonidin
-
-
petunidin
-
-
Pyridine
-
non-competitive inhibition of mutant E218A by pyridine
quercetagetin
-
-
quercetagetinidin
-
-
quercetin
-
-
robinetin
-
-
Sn2+
-
complete inhibition at 2 mM; inhibition of NADase and adenosine diphosphate cyclase
Zn2+
-
; inhibition of NADase and adenosine diphosphate cyclase
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.851
3-acetylpyridine adenine dinucleotide
-
-
0.046
beta-NAD+
-
-
0.224
cyclic ADP-ribose
-
-
0.007
epsilon-NAD+
-
-
0.033
epsilonNAD+
-
-
0.0171 - 1.33
NAD+
0.065 - 0.66
NADP+
0.033
nicotinamide 1,N6-ethenoadenine dinucleotide
-
pH 7.0, 28C
0.0016
nicotinamide guanine dinucleotide
-
-
1.44
nicotinamide-hypoxanthine dinucleotide
-
-
0.51
nicotinamide-hypoxanthine dinucleotide phosphate
-
-
-
0.25
thio-NAD+
-
-
additional information
additional information
-
steady state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0155 - 57.9
NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54 - 3380
NAD+
7
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0321
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)chromenium
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0218
cyanidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0146
delphinidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0703
fisetinidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0063
kuromanin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0082
luteolin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.006
luteolinidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.017
malvidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0248
myricetin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0163
pelargonidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0209
peonidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0392
petunidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0486
quercetagetin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0142
quercetagetinidin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0379
quercetin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0379
robinetin
Homo sapiens
-
at 37C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
partially purified enzyme, ADPR activity
0.0604
NAD+-glycohydrolase activityin crude cell extract, pH 7.4, 37C
0.113
-
partially purified enzyme, cADPR activity
2.205
-
partially purified enzyme, NADase activity
409
-
NAD(P)ase II
662
-
NAD(P)ase I
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
citrate buffer, activity is essentially unchanged
6 - 10
-
phosphate buffer, activity is essentially unchanged
7
-
; NADase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38 - 50
-
inactive above 50C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
isoelectric focusing
6.4 - 6.6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
surface antigen CD38
Manually annotated by BRENDA team
-
activity is 4times higher in Burkitt's lymphoma-derived cell lines than in nonmalignant control lines
Manually annotated by BRENDA team
-
the enzyme is the leucocyte antigen CD38
Manually annotated by BRENDA team
-
primary microglial cultures as cellular models
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
surface antigen CD38
-
Manually annotated by BRENDA team
mitochondrial membrane
Manually annotated by BRENDA team
-
CD38 is predominately on the plasma membrane of Raji and retinoic acid-treated HL-60 cells
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23500
-
gel filtration
28970
x * 45000, SDS-PAGE, x * 28970, sequence calculation
38000
-
gel filtration
39000
-
1 * 39000, SDS-PAGE
50000
-
NAD(P)ase I, gel filtration
1600000
-
gel filtration
additional information
-
native enzyme shows high molecular weight and elutes in the void volumes from a Superose 12 gel filtration column
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45000, SDS-PAGE, x * 28970, sequence calculation
monomer
-
1 * 39000, SDS-PAGE
oligomer
-
x * 45000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mono N-glycosylated forms of soluble enzyme ecto-domain (residues 32-278) and catalytic residue mutant Glu218Gln, in apo state or bound to 2'-fluorinated NAD+ derivatives aFNAD or rFNAD, hanging drop vapour diffusion method, from 20-30% PEG 4000, 50-250 mM ammonium sulfate and 100 mM sodium cacodylate, sodium acetate or MES, pH 6.0-6.5, room temperature, soaking of crystals in 1-3 mM ligand solution, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement
-
enzyme in complex with inhibitors, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM HEPES with 5 mm ligands, with reservoir solution containing 0.1 M sodium acetate, pH 4.0, 0.2 M ammonium acetate, 3% 2-propanol, and 15% PEG 10000, X-ray diffraction structure determination and analysis, molecular replacement
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 10
-
5 min, 50 mM citrate, stable
326404
3 - 11
-
25C, 10 min, stable
326403
4 - 5
-
5 min, less than 10% loss of activity
326404
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
5 min, 20% loss of activity
38
-
half-life: about 1 day
50
-
5 min, complete inactivation
60
-
rapid loss of activity above
100
-
60% loss of activity after 30 min, 80% loss of activity after 1 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% inactivation at 2 M urea
-
SDS, even at micromolar concentration, leads to complete inactivation of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several weeks
-
20C, lyophilized enzyme, 90% remaining activity after 6 months
-
4C to -196C, 10 mM Tris-HCl, pH 8.0, 0.1% Triton X-100, at least 1 month, stable
-
4C, -20C, -80C or -196C, pH 8.0, 0.1% Triton X-100, 10 mM Tris-HCl, stable for at least 1 month
-
4C, 0.1 M Tris-HCl buffer, pH 7.0, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD(P)ase I and II
-
native enzyme 480fold from serum by ammonium sulfate fractionation, affinity chromatography, gel filtration, and isoelectric focusing, and again gel filtration, to homogeneity
-
partial
partial; partially from spleen microsomal membranes after solubilization with Triton X-100, chromatography methods, 133fold
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cd38, eight exons, DNA and amino acid sequence determination and analysis, sequence comparison to the human enzyme, phylogenetic tree, expression in COS-7 cells
recombinant expression of bovine CD38/NAD+ glycohydrolase truncated for the first 31 amino acids that encompass the transmembrane and short intracellular domains in Pichia pastoris. The construct comprises a DNA fragment encoding the ecto-domain in the expression plasmid pPICZaA in frame with the yeast alpha-factor secretion signal sequence under the transcriptional control of the AOX1 promoter and keeping its original stop codon
-
the soluble ecto-domain of human CD38 is expressed in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.001 mM ATRA induces CD38 expression
-
enzyme induction by retinoic acid in HL-60 cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D147A
-
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
E138A
-
site-directed mutagenesis, the mutation causes a modest increase in the rate of NAD+ transformation which is proportional to its concentration. At 4.0 M, the rate increase is about 1.2fold and the formation of beta-1'-O-methyl ADP-ribose amounts to about 80% of the total reaction products. The observed selectivity in favor of methanolysis is similar to that of wild-type enzyme. The ADP-ribosyl cyclase activity of E138A mutant is more affected by the competing nucleophile, i.e. formation of ADP-ribose and cADPR are reduced by 75% and 90% respectively at 4.0 M methanol, the mutant shows an increase in ADP cyclization and higly reduced overall activity compared to the wild-type enzyme
E138Q
-
site-directed mutagenesis, in the presence of methanol, mutant E138Q efficiently catalyzes the formation of beta-1'-O-methyl ADP-ribose. But in contrast with mutant E138A, and like the wild-type enzyme, solvolysis does not affect the overall turnover rate of NAD+ indicating that the formation of the E.ADP-ribosyl intermediate is still rate limiting
E218A
-
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
K120A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R216A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S185A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W118A
-
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate compared to the wild-type enzyme
W118A/W181A
-
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate which is 16fold lower than the product of the effects of the two single mutations
W118F
-
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
W118H
-
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
W168A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W181A
-
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate and a reduced sensitivity to nicotinamide inhibition compared to the wild-type enzyme
W181F
-
site-directed mutagenesis, the mutant shows a decrease in activity and an increase in ADP cyclization compared to the wild-type enzyme
N100D
-
site-directed mutagenesis, N-glycoylation at the site is abolished
N164D
-
site-directed mutagenesis, N-glycoylation at the site is abolished
N209D
-
site-directed mutagenesis, N-glycoylation at the site is abolished
N219D
-
site-directed mutagenesis, N-glycoylation at the site is abolished
additional information
-
construction of CD38/NAD+ glycohydrolase truncated for the first 31 amino acids that encompass the transmembrane and short intracellular domains
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
80% renaturation of urea and SDS denatured enzyme by treatment with Triton X-100 in a 20:1 v/w ratio with SDS
-