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Information on EC 2.1.1.5 - betaine-homocysteine S-methyltransferase and Organism(s) Rattus norvegicus and UniProt Accession O09171
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EC Tree
2.1.1.5 betaine-homocysteine S-methyltransferaseSpecify your search results
Word Map
- 2.1.1.5
- cystathionine
- s-adenosylmethionine
- choline
- folate
-
remethylation
- hyperhomocysteinemia
- s-adenosylhomocysteine
-
adenosyltransferase
- n-methyltransferase
-
one-carbon
- beta-synthase
- dimethylglycine
-
transsulfuration
- methylenetetrahydrofolate
-
5-methyltetrahydrofolate-homocysteine
-
transmethylation
- medicine
- mthfd1
- guanidinoacetate
-
homocysteine-induced
-
folate-dependent
- homocystinuria
- 5-methyltetrahydrofolate
-
transcobalamin
-
b-vitamins
-
slc19a1
- hypotaurine
- molecular biology
- analysis
- nutrition
- food industry
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
betaine-homocysteine methyltransferase, betaine-homocysteine s-methyltransferase, betaine homocysteine methyltransferase, bhmt2, betaine:homocysteine methyltransferase, bhmt-2, bhmt1, betaine homocysteine s-methyltransferase, betaine-homocysteine s-methyltransferase 2, betaine:homocysteine s-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
betaine-homocysteine methyltransferase
betaine-homocysteine transmethylase
-
-
-
-
BHMT
methyltransferase, betaine-homocysteine
-
-
-
-
betaine-homocysteine methyltransferase
-
-
-
-
BHMT
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
betaine + L-homocysteine = dimethylglycine + L-methionine
ordered bi-bi mechanism with homocysteine the first substrate to be added and methionine the last product released
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
trimethylammonioacetate:L-homocysteine S-methyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9029-78-1
-
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-homocysteine + betaine
L-methionine + dimethylglycine
-
-
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
reduced BHMT activity in cirrhotic livers may explain the elevated plasma homocysteine levels in cirrhosis
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
folate-independent remethylation of homocysteine
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
this reaction processes 25% of the cellular L-homocysteine in an in vitro model
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
i.e. betaine, involved in betaine metabolism
-
-
?
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
L-homocysteine + betaine
L-methionine + dimethylglycine
-
reduced BHMT activity in cirrhotic livers may explain the elevated plasma homocysteine levels in cirrhosis
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
i.e. betaine, involved in betaine metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
actinomycin D
leads to a decay of Bhmt mRNA, irrespective of the ambient osmolarity, at 120 min after addition, Bhmt mRNA levels are significantly decreased under hyperosmotic conditions, compared with the Bhmt mRNA levels found under the respective normo- or hypoosmotic condition
S-adenosyl-L-ethionine
-
irreversible, S-adenosyl-L-homocysteine and L-homocysteine prevent, but not DL-homocysteine, GSH, DTT or L-cysteine
S-adenosyl-L-homocysteine
-
non-linear/competitive to homocysteine, mixed/non-competitive to betaine
S-adenosyl-L-methionine
-
irreversible, S-adenosyl-L-homocysteine and L-homocysteine prevent, not DL-homocysteine, GSH, DTT or L-cysteine
additional information
-
hyperosmotic NaCl, hyperosmotic raffinose but not hyperosmotic urea suppresses Bhmt mRNA expression, suggesting that cell shrinkage rather than increased ionic strength or hyperosmolarity per se is the trigger, osmosensitivity of Bhmt mRNA expression is impaired by inhibitors of tyrosine kinases and cyclic nucleotide-dependent kinases
-
additional information
hyperosmotic NaCl, hyperosmotic raffinose but not hyperosmotic urea suppresses Bhmt mRNA expression, suggesting that cell shrinkage rather than increased ionic strength or hyperosmolarity per se is the trigger, osmosensitivity of Bhmt mRNA expression is impaired by inhibitors of tyrosine kinases and cyclic nucleotide-dependent kinases
-
additional information
-
not inhibitory: taurine, cysteic acid, cysteine sulfinate, sulfate, glycine, L-serine, L-threonine
-
additional information
-
insulin decreases the abundance of BHMT mRNA and the rate of de novo mRNA transcription of the gene in H4IIE cells, plays a direct role in the regulation of BHMT transcription
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Insulin
-
is effective in counteracting the stimulation of BHMT activity and mRNA levels produced by triamcinolone in rat hepatoma H4IIE cells
-
L-methionine
-
independent of dietary choline, supplemental methionine increases hepatic BHMT activity by ca. 30%
betaine
-
together with methionine restriction induces hepatic BHMT 4fold compared with methionine restriction alone, BHMT mRNAlevel is also increased by 3fold by betaine supplementation of methionine-replete diets
choline
-
liver BHMT activity is 1.3fold higher in rats fed the methionine deficient diet containing choline than in rats fed the methionine-adequate diet containing supplemental choline
additional information
-
after 24 h, Bhmt expression increases 1.53fold under hypoosmotic conditions, Bhmt enzymatic activity is altered under anisoosmotic conditions
-
additional information
after 24 h, Bhmt expression increases 1.53fold under hypoosmotic conditions, Bhmt enzymatic activity is altered under anisoosmotic conditions
-
additional information
-
taurine, cysteic acid, cysteine sulfinate, sulfate, glycine, L-serine, L-threonine do not affect activity
-
additional information
-
choline and methionine do not affect BHMT activity, mRNA expression and immunodetectable protein in the kidney
-
additional information
-
diet increases BHMT activity with small elevations in expression
-
additional information
-
triamcinolone increases the level and rate of BHMT mRNA synthesis in H4IIE cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
hyperosmolarity (405 mosmol/l) suppresses Bhmt mRNA expression whereas hypoosmotic (205 mosmol/l) conditions induce Bhmt mRNA expression. Like hyperosmotic NaCl, hyperosmotic raffinose but not hyperosmotic urea suppresses Bhmt mRNA expression. Osmosensitivity of Bhmt mRNA expression is impaired by inhibitors of tyrosine kinases and cyclic nucleotide-dependent kinases
-
-
-
reduced BHMT activity in cirrhotic livers may explain the elevated plasma homocysteine levels in cirrhosis
-
BHMT mRNA and activity increases about 2fold in diabetic rats compared with the nondiabetic animals
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
identification of interactions of betaine homocysteine S-methyltransferase in normal liver. S-methylmethionine homocysteine methyltransferase or betaine homocysteine methyltransferase 2, methionine adenosyltransferases alpha1 and alpha2, cAMP-dependent protein kinase catalytic subunit alpha, 4-hydroxyphenylpyruvic acid dioxygenase and aldolase b. Network analysis identified 122 nodes and 165 edges, as well as a limited number of KEGG pathways that comprise the biosynthesis of amino acids, cysteine and methionine metabolism, the spliceosome and metabolic pathways
physiological function
-
in rats fed methionine and choline-deficient diet, betaine supplementation reverses the reduction of methionine and S-adenosylmethionine, and the elevation of homocysteine levels in the liver, due to the induction of betaine-homocysteine methyltransferase and methionine adenosyltransferase MAT
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). BHMT1_RAT
407
0
44976
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals with P2(1) symmetry, assymetric unit contains the whole functional tetramer showing point symmetry 222
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A119G
1.9fold reduced turnover-number for betaine and L-homocysteine, 1.6fold reduced KM-value for L-homocysteine, 1.1fold decrease in Km-value for betaine
C186A
1.8fold reduced turnover-number for betaine and L-homocysteine, 4.3fold reduced KM-value for L-homocysteine, 1.8fold increase in Km-value for betaine
C186S
2.3fold reduced turnover-number for betaine and L-homocysteine, 1.4fold reduced KM-value for L-homocysteine, 111.6fold decrease in Km-value for betaine
D26A
2.7fold reduced turnover-number for betaine and L-homocysteine, 1.7fold reduced KM-value for L-homocysteine, 3.5fold increase in Km-value for betaine
D26I
67fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 6.5fold lower than the wild-type value
E159G
60fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 61.2fold lower than the wild-type value
E159K
170fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 169.7fold lower than the wild-type value
E21A
2.3fold reduced turnover-number for betaine and L-homocysteine, 6fold reduced KM-value for L-homocysteine, 2.4fold reduced Km-value for betaine
E21K
1.6fold reduced turnover-number for betaine and L-homocysteine, 1.4fold reduced KM-value for L-homocysteine, 1.7fold reduced Km-value for betaine
F74A
1.9fold reduced turnover-number for betaine and L-homocysteine, 1.9fold reduced KM-value for L-homocysteine, 2.9fold increase in Km-value for betaine
T184G
2.4fold reduced turnover-number for betaine and L-homocysteine, 3.19fold reduced KM-value for L-homocysteine, 1.6fold increase in Km-value for betaine
T73G
3.1fold reduced turnover-number for betaine and L-homocysteine, 2.2fold reduced KM-value for L-homocysteine, 1.3fold reduced Km-value for betaine
Y77A
14fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 13.7fold lower than the wild-type value
additional information
-
changes at positions E159 and Y77 show the largest decreases in activity, but D26 and F74 seem to have a role in betaine binding, whereas E21 and C186 also influence L-homocysteine binding
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
mechanism of unfolding by urea includes two intermediate states, a tetramer and a monomer. Dissociation is concomitant with alterations in the dimerization arm and the loop connecting the C-terminal helix, and intermediate conformations originate from perturbations in these structures
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
corticosteroids stimulate activity in the liver and also up-regulate the gene expression
-
significant upregulation of betaine homocysteine methyltransferase-1 in livers of rats fed a betaine supplemented ethanol diet
-
the activity of hepatic BHMT significantly increases with increase in both dietary casein level and dietary methionine level, hepatic level of mRNA for BHMT is parallel to the enzyme activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
osmotic regulation of BHMT may be part of a cell volume-regulatory response and additionally lead to metabolic alterations that depend on the availability of betaine-derived methyl groups
nutrition
-
rats fed a casein-based diet lacking folate exhibit a 53% increase in circulating homocysteine concentrations compared with rats fed a casein-based diet including folate. Serum homocysteine does not differ between rats fed casein-based diet including folate and egg protein-based diet lacking folate. Hepatic BHMT activity is increased by 45% and 40% by the egg protein-based diet and whole egg-based diet compared with the casein-based diets, respectively
additional information
medicine
-
decreased plasma homocysteine in various models of diabetes may be due to enhanced homocysteine removal brought about by a combination of increased transsulfuration of homocysteine to cysteine and increased remethylation of homocysteine to methionine by BHMT
medicine
-
upregulation of BHMT may indicate an increased choline requirement in the diabetic rat
medicine
-
Zucker diabetic fatty rats show increased BHMT activity and mRNA levels
additional information
-
Bhmt expression is strongly regulated by changes in ambient osmolarity, osmotic regulation of BHMT may be part of a cell volume-regulatory response and additionally leads to metabolic alterations that depend on the availability of betaine-derived methyl groups
additional information
Bhmt expression is strongly regulated by changes in ambient osmolarity, osmotic regulation of BHMT may be part of a cell volume-regulatory response and additionally leads to metabolic alterations that depend on the availability of betaine-derived methyl groups
additional information
-
relationship between BHMT expression and ApoB mRNA in transfected McA cells recapitulated in vivo through dietary BHMT induction, providing additional support for a physiologic linkage between 1-carbon metabolism and apob gene expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Finkelstein, J.D.; Harris, B.J.; Kyle, W.E.
Methionine metabolism in mammals: kinetic study of betaine-homocysteine methyltransferase
Arch. Biochem. Biophys.
153
320-324
1972
Rattus norvegicus
Lee, K.H.; Cava, M.; Amiri, P.; Ottoboni, T.; Lindquist, R.N.
Betaine:homocysteine methyltransferase from rat liver: purification and inhibition by a boronic acid substrate analog
Arch. Biochem. Biophys.
292
77-86
1992
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Finkelstein, J.D.; Martin, J.J.
Inactivation of betaine-homocysteine methyltransferase by adenosylmethionine and adenosylethionine
Biochem. Biophys. Res. Commun.
118
14-19
1984
Rattus norvegicus
Finkelstein, J.D.; Kyle, W.E.; Harris, B.J.
Methionine metabolism in mammals: regulatory effects of S-adenosylhomocysteine
Arch. Biochem. Biophys.
165
774-779
1974
Rattus norvegicus
Gonzalez, B.; Pajares, M.A.; Too, H.P.; Garrido, F.; Blundell, T.L.; Sanz-Aparicio, J.
Crystallization and preliminary x-ray study of recombinant betaine-homocysteine S-methyltransferase from rat liver
Acta Crystallogr. Sect. D
58
1507-1510
2002
Rattus norvegicus
Delgado-Reyes, C.V.; Wallig, M.A.; Garrow, T.A.
Immunohistochemical detection of betaine-homocysteine S-methyltransferase in human, pig, and rat liver and kidney
Arch. Biochem. Biophys.
393
184-186
2001
Homo sapiens, Rattus norvegicus, Sus scrofa
Gonzalez, B.; Campillo, N.; Garrido, F.; Gasset, M.; Sanz-Aparicio, J.; Pajares, M.A.
Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
Biochem. J.
370
945-952
2003
Rattus norvegicus (O09171)
Garrido, F.; Gasset, M.; Sanz-Aparicio, J.; Alfonso, C.; Pajares, M.A.
Rat liver betaine homocysteine S-methyltransferase equilibrium unfolding: insights into intermediate structure through tryptophan substitutions
Biochem. J.
391
589-599
2005
Rattus norvegicus
Forestier, M.; Banninger, R.; Reichen, J.; Solioz, M.
Betaine homocysteine methyltransferase: gene cloning and expression analysis in rat liver cirrhosis
Biochim. Biophys. Acta
1638
29-34
2003
Rattus norvegicus
Gonzalez, B.; Pajares, M.A.; Martinez-Ripoll, M.; Blundell, T.L.; Sanz-Aparicio, J.
Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding
J. Mol. Biol.
338
771-782
2004
Rattus norvegicus (O09171)
Ratnam, S.; Wijekoon, E.P.; Hall, B.; Garrow, T.A.; Brosnan, M.E.; Brosnan, J.T.
Effects of diabetes and insulin on betaine-homocysteine S-methyltransferase expression in rat liver
Am. J. Physiol. Endocrinol. Metab.
290
E933-E939
2006
Rattus norvegicus
Nieman, K.M.; Hartz, C.S.; Szegedi, S.S.; Garrow, T.A.; Sparks, J.D.; Schalinske, K.L.
Folate status modulates the induction of hepatic glycine N-methyltransferase and homocysteine metabolism in diabetic rats
Am. J. Physiol. Endocrinol. Metab.
291
E1235-E1242
2006
Rattus norvegicus
Schaefer, C.; Hoffmann, L.; Heldt, K.; Lornejad-Schaefer, M.R.; Brauers, G.; Gehrmann, T.; Garrow, T.A.; Haeussinger, D.; Mayatepek, E.; Schwahn, B.C.; Schliess, F.
Osmotic regulation of betaine homocysteine-S-methyltransferase expression in H4IIE rat hepatoma cells
Am. J. Physiol. Gastrointest. Liver Physiol.
292
G1089-G1098
2007
Mus musculus, Rattus norvegicus, Rattus norvegicus (O09171)
Sparks, J.D.; Collins, H.L.; Chirieac, D.V.; Cianci, J.; Jokinen, J.; Sowden, M.P.; Galloway, C.A.; Sparks, C.E.
Hepatic very-low-density lipoprotein and apolipoprotein B production are increased following in vivo induction of betaine-homocysteine S-methyltransferase
Biochem. J.
395
363-371
2006
Rattus norvegicus
Pajares, M.A.; Perez-Sala, D.
Betaine homocysteine S-methyltransferase: just a regulator of homocysteine metabolism?
Cell. Mol. Life Sci.
63
2792-2803
2006
Cavia porcellus, Homo sapiens, Macaca mulatta, Mesocricetus auratus, Mus musculus, Mus musculus C57/BL6J, Ovis aries, Rattus norvegicus, Sus scrofa
Slow, S.; Garrow, T.A.
Liver choline dehydrogenase and kidney betaine-homocysteine methyltransferase expression are not affected by methionine or choline intake in growing rats
J. Nutr.
136
2279-2283
2006
Rattus norvegicus
Kharbanda, K.K.; Vigneswara, V.; McVicker, B.L.; Newlaczyl, A.U.; Bailey, K.; Tuma, D.; Ray, D.E.; Carter, W.G.
Proteomics reveal a concerted upregulation of methionine metabolic pathway enzymes, and downregulation of carbonic anhydrase-III, in betaine supplemented ethanol-fed rats
Biochem. Biophys. Res. Commun.
381
523-527
2009
Rattus norvegicus
Ohuchi, S.; Morita, T.; Mori, M.; Sugiyama, K.
Hepatic cystathionine beta-synthase activity does not increase in response to methionine supplementation in rats fed a low casein diet: association with plasma homocysteine concentrations
J. Nutr. Sci. Vitaminol.
55
178-185
2009
Rattus norvegicus
Fridman, O.; Morales, A.V.; Bortoni, L.E.; Turk-Noceto, P.C.; Prieto, E.A.
Corticoadrenal activity in rat regulates betaine-homocysteine S-methyltransferase expression with opposite effects in liver and kidney
J. Biosci.
37
115-123
2012
Rattus norvegicus
Ahn, C.W.; Jun, D.S.; Na, J.D.; Choi, Y.J.; Kim, Y.C.
Alleviation of hepatic fat accumulation by betaine involves reduction of homocysteine via up-regulation of betaine-homocysteine methyltransferase (BHMT)
Biochem. Biophys. Res. Commun.
477
440-447
2016
Rattus norvegicus
Saande, C.J.; Pritchard, S.K.; Worrall, D.M.; Snavely, S.E.; Nass, C.A.; Neuman, J.C.; Luchtel, R.A.; Dobiszewski, S.; Miller, J.W.; Vailati-Riboni, M.; Loor, J.J.; Schalinske, K.L.
Dietary egg protein prevents hyperhomocysteinemia via upregulation of hepatic betaine-homocysteine S-methyltransferase activity in folate-restricted rats
J. Nutr.
149
1369-1376
2019
Rattus norvegicus
Garrido, F.; Pacheco, M.; Vargas-Martinez, R.; Velasco-Garcia, R.; Jorge, I.; Serrano, H.; Portillo, F.; Vazquez, J.; Pajares, M.A.
Identification of hepatic protein-protein interaction targets for betaine homocysteine S-methyltransferase
PLoS ONE
13
e0199472
2018
Rattus norvegicus (O09171), Rattus norvegicus
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