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Information on EC 2.7.6.1 - ribose-phosphate diphosphokinase and Organism(s) Rattus norvegicus
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2.7.6.1 ribose-phosphate diphosphokinaseIUBMB Comments
dATP can also act as donor.
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Word Map
- 2.7.6.1
- purine
- erythrocyte
-
superactivity
- pyrimidine
-
x-linked
- phosphoribosyltransferase
-
uric
- gout
- hypoxanthine
-
hypoxanthine-guanine
- deafness
- charcot-marie-tooth
-
sensorineural
-
hemolysates
-
diphosphorylated
-
nonsyndromic
- hgprt
-
hyperuricaemia
- lesch-nyhan
-
phosphoribosyl-pyrophosphate
-
feedback-resistant
- synthesis
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
prps1, prpp synthetase, phosphoribosylpyrophosphate synthetase, phosphoribosyl pyrophosphate synthetase, prpp synthase, prpps, prs-i, ribose-phosphate pyrophosphokinase, ppribp synthetase, 5-phosphoribosyl-1-pyrophosphate synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-phosphoribose pyrophosphorylase
-
-
-
-
5-phosphoribosyl-1-pyrophosphate synthetase
-
-
-
-
5-phosphoribosyl-alpha-1-pyrophosphate synthetase
-
-
-
-
ATP:D-ribose-5-phosphate pyrophosphotransferase
-
-
-
-
phosphoribosyl-diphosphate synthetase
-
-
-
-
phosphoribosylpyrophosphate synthase
-
-
-
-
phosphoribosylpyrophosphate synthetase
-
-
-
-
PP-ribose P synthetase
-
-
-
-
PPRibP synthetase
-
-
-
-
PRPP synthase
-
-
-
-
PRPP synthetase
-
-
-
-
pyrophosphokinase, ribose phosphate
-
-
-
-
pyrophosphoribosylphosphate synthetase
-
-
-
-
ribophosphate pyrophosphokinase
-
-
-
-
ribose-5-phosphate pyrophosphokinase
-
-
-
-
ribose-phosphate pyrophosphokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diphosphate transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose-5-phosphate diphosphotransferase
dATP can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY
9015-83-2
-
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
(R)9-(2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(R)9-(2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
-
-
-
r
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
-
-
-
r
(S)9-(2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(S)9-(2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
-
-
-
r
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
-
-
-
r
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate + 5-phospho-alpha-D-ribose 1-diphosphate
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-triphosphate + D-ribose 5-phosphate
-
-
-
r
9-(2-phosphonylmethoxyethoxy)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethoxy)adenine-diphosphate + D-ribose 5-phosphate
-
-
-
r
9-(2-phosphonylmethoxyethyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethyl)adenine-diphosphate + D-ribose 5-phosphate
-
-
-
r
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + D-ribose 5-phosphate
-
-
-
r
ATP + 6-deoxyhomoribose 6-phosphonate
AMP + 6-deoxyhomoribose 6-phosphonate 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphothionate
AMP + 5-phosphotionate-alpha-D-ribose 1-diphosphate
-
-
-
r
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
highly specific for D-ribose 5-phosphate
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
highly specific for D-ribose 5-phosphate
ribose product also known as 5-phosphoryl-D-ribofuranose alpha-1-diphosphate
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
slightly more effective than ATP
-
r
additional information
?
-
-
ribose, ribose-1-phosphate, deoxyribose-5-phosphate, glucose-6-phosphate are not effective as substrates
-
-
?
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
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
Mg2+
-
required to form a complex with ATP and as a free cation
additional information
-
absolute requirement for a divalent cation for activity
additional information
-
absolute requirement for a divalent cation for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PRPP synthetase-associated proteins
-
inhibit catalytic and perhaps regulatory functions of the enzyme
-
TDP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells, competitive with respect to ATP
ADP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells
ADP
-
when PAP39 complexes with PRSI or PRSII, the sensitivity to ADP inhibition is lowered
AMP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells, competitive with respect to ATP
GDP
-
when PAP39 complexes with PRSI or PRSII, the sensitivity to ADP inhibition is lowered
nucleotides
-
enzyme from HTC cells has an altered sensitivity to feedback inhibition by purine and pyrimidine nucleotides
-
additional information
-
native enzyme is less sensitive to nucleotide inhibition than the major component of the enzyme, rPRSI
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
at 50 and 100 mM, KCl, KHCO3 and CH3COOK have no activating effects
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.923
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37ºC, isoenzyme I
3.636
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37ºC, isoenzyme I
0.317
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37ºC, isoenzyme II
0.323
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37ºC, isoenzyme I
0.0289
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37ºC, native enzyme from liver
0.0402
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37ºC, isoenzyme rPRSII
0.0418
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37ºC, isoenzyme rPRSI
0.29
5-phospho-D-ribose diphosphate
-
pH and temperature conditions not mentioned
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the specific activity of the catalytic subunit is lower in the complexes where the amount of PRPP synthetase-associated protein of 39000 Da, PAP39, is higher. Increasing amounts of PAP39 have strong inhibitory effects on the catalytic activity
additional information
-
33400 U/mg and 46200 U/mg for PRSI and PRSII purified isoenzymes, respectively
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cell line of rat hepatoma cells in continuous culture, clone MAU V with an inreased ability to salvage exogenous purines
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
60% of the total activity, fractionation by discontinuous sucrose density gradient centrifugation
-
30% of the total activity, fractionation by discontinuous sucrose density gradient centrifugation
-
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). PRPS1_RAT
318
0
34834
Swiss-Prot
other Location (Reliability: 2)
PRPS2_RAT
318
0
34813
Swiss-Prot
other Location (Reliability: 3)
A0A0G2JSV3_RAT
318
0
34806
TrEMBL
other Location (Reliability: 2)
M0RBK1_RAT
318
0
34852
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1000000
34000
38000
-
x * 34000 + x * 38000 + x * 40000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit
39000
-
x * 34000 + x * 39000 + x * 41000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit which appears as PRSI or PRSII
40000
41000
-
x * 34000 + x * 39000 + x * 41000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit which appears as PRSI or PRSII
700000 - 1200000
additional information
34000
-
x * 34000 + x * 39000 + x * 41000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit which appears as PRSI or PRSII
34000
-
x * 34000 + x * 38000 + x * 40000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit
40000
-
x * 34000 + x * 38000 + x * 40000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit
additional information
-
the catalytic subunit complexes with the PRPP synthetase-associated protein of 39000 Da, PAP39, to form highly aggregated forms
additional information
-
the catalytic subunit complexes with the PRPP synthetase-associated protein of 39000 Da, PAP39, to form highly aggregated forms
additional information
-
purified enzyme appears to exist as complex aggregates composed of heterogeneous components
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 34000 + x * 39000 + x * 41000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit which appears as PRSI or PRSII
?
-
x * 34000 + x * 38000 + x * 40000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49
49
-
half-life of 0.5 min and 90 min for isoenzymes rPRSII and rPRSI, respectively
49
-
half-life of 250 min, 90 min and 0.5 min for native enzyme, isoenzymes rPRSI and rPRSII, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of albumin, EDTA or sulfhydryl compounds to the assay prevents loss of activity
-
high enzyme concentration, albumin, 0.05 mg/ml, EDTA, 1 mM or DTT, 1 mM stabilizes during assay
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4ºC, 50% loss of activity after 2 months. -20ºC, more rapid loss of activity. Presence of substrates enhances stability during storage
-
4ºC, without stabilizing agents, half-life of inactivation of 21, 8 and 1 hours for native enzyme, isoenzymes rPRSI and rPRSII, respectively
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
acetone powder, acid and streptomycin precipitation, ammonium sulfate fractionation, heat treatment and agarose gel filtration, 3400fold purification, presence of substrates enhances stability during purification
-
acetone powder, acid and streptomycin precipitation, heat treatment and agarose chromatography, 1500 to 3000fold purification
-
polyethylene glycol precipitation, hydroxyapatite fractionation, gel filtration on Toyopearl HW-65F, chromatography on DEAE-Toyopearl 650S and gel filtration
-
polyethylene glycol, acid precipitation and chromatography on DEAE-5PW HPLC, purification of the two isoforms PRSI and PRSII
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Switzer, R.L.
Phosphoribosylpyrophosphate synthetase and related pyrophosphokinases
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
10
607-629
1974
Gallus gallus, Columba sp., Escherichia coli, Homo sapiens, Mus musculus, Ophiodon elongatus, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
-
Roth, D.G.; White, C.; Deuel, T.F.
Ribosephosphate pyrophosphokinase (rat liver)
Methods Enzymol.
51
12-17
1978
Rattus norvegicus
Ishijima, S.; Kita, K.; Ahmad, I.; Ishizuka, T.; Taira, M.; Tatibana, M.
Expression of rat phosphoribosylpyrophosphate synthetase subunits I and II in Escherichia coli. Isolation and characterization of the recombinant isoforms
J. Biol. Chem.
266
15693-15697
1991
Rattus norvegicus
Roth, D.G.; Shelton, E.; Deuel, T.F.
Purification and properties of phosphoribosyl pyrophosphate synthetase from rat liver
J. Biol. Chem.
249
291-296
1974
Rattus norvegicus
Kita, K.; Otsuki, T.; Ishizuka, T.; Tatibana, M.
Rat liver phosphoribosyl pyrophosphate synthetase: existence of the purified enzyme as heterogeneous aggregates and identification of the catalytic subunit
J. Biochem.
105
736-741
1989
Rattus norvegicus
Green, C.D.; Martin, D.W.
Characterization of a feedback-resistant phosphoribosylpyrophosphate synthetase from cultured, mutagenized hepatoma cells that overproduce purines
Proc. Natl. Acad. Sci. USA
70
3698-3702
1973
Rattus norvegicus
Balzarini, J.; Nave, J.F.; Becker, M.A.; Tatibana, M.; De Clercq, E.
Kinetic properties of adenine nucleotide analogs against purified 5-phosphoribosyl-1-pyrophosphate synthetase from E. coli, rat liver and human erythrocytes
Nucleosides Nucleotides
14
1861-1871
1995
Escherichia coli, Homo sapiens, Rattus norvegicus
-
Sonoda, T.; Kita, K.; Ishijima, S.; Ishizuka, T.; Ahmad, I.; Tatibana, M.
Kinetic and regulatory properties of rat liver phosphoribosylpyrophosphate synthetase complex are partly distinct from those of isolated recombinant component catalytic subunits
J. Biochem.
122
635-640
1997
Rattus norvegicus
Ishijima, S.; Asai, T.; Kita, K.; Sonoda, T.; Tatibana, M.
Partial reconstitution of mammalian phosphoribosylpyrophosphate synthetase in Escherichia coli cells. Coexpression of catalytic subunits with the 39-kDa associated protein leads to formation of soluble multimeric complexes of various compositions
Biochim. Biophys. Acta
1342
28-36
1997
Rattus norvegicus
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