Any feedback?
No. of entries
Information on EC 2.7.7.47 - streptomycin 3''-adenylyltransferase
for references in articles please use BRENDA:EC2.7.7.47
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.47 streptomycin 3''-adenylyltransferase
IUBMB Comments
Also acts on spectinomycin.
The enzyme appears in viruses and cellular organisms
- 2.7.7.47
- integrons
- medicine
-
aminoglycoside-modifying
- blavim-2
-
streptomycin-resistant
-
dfra15
- diagnostics
- agriculture
- analysis
Synonyms
aminoglycoside adenyltransferase, aminoglycoside adenylyltransferase, streptomycin adenylyltransferase, aada6, aminoglycoside 3'-adenyltransferase, smatase, streptomycin adenyltransferase, aminoglycoside adenyltransferase type a, aminoglycoside adenyltransferase a, ant(3'')-ii, more
top
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAD (3'')
-
-
-
-
aadA
AadA6
aminoglycoside 3''-adenylyltransferase
aminoglycoside 3'-adenyltransferase
aminoglycoside adenyltransferase
aminoglycoside adenyltransferase A
aminoglycoside adenyltransferase type A
ANT(3'')-II
str
streptomycin adenylate synthetase
-
-
-
-
streptomycin adenyltransferase
-
-
-
-
streptomycin adenylylase
-
-
-
-
streptomycin adenylyltransferase
streptomycin-spectinomycin adenylyltransferase
-
-
-
-
aminoglycoside 3''-adenylyltransferase
-
-
-
-
aminoglycoside 3'-adenyltransferase
-
aadA is used as marker gene in gene modified crop
aminoglycoside adenyltransferase
-
types aadA1, aadA2, aadA5, aadA7, aadA23, aac3-Id
aminoglycoside adenyltransferase A
-
aminoglycoside adenyltransferase A
-
-
aminoglycoside adenyltransferase type A
-
-
aminoglycoside adenyltransferase type A
-
-
streptomycin adenylyltransferase
-
-
-
-
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
ATP + streptomycin = diphosphate + 3''-adenylylstreptomycin
also acts on sprctionomycin
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:streptomycin 3''-adenylyltransferase
Also acts on spectinomycin.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
52660-23-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + bluensomycin
diphosphate + 3''-adenylylbluensomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptobiosamine
diphosphate + 3''-adenylylstreptobiosamine
-
Substrates: degradation product streptomycin
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Acinetobacter sp. NIPH 758 (IIb)
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: inactivation of the antibiotic by adenylating the 9-hydroxyl-group
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: inactivation of the antibiotic by adenylating the 9-hydroxyl-group
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Acinetobacter sp. NIPH 758 (IIb)
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: enzyme leads to resistance, destroys the inhibitory activity of streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: enzyme leads to resistance, destroys the inhibitory activity of streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: enzyme leads to resistance, destroys the inhibitory activity of streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: important mechanism of streptomycin modification is through ATP-dependent O -adenylation
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: sequential mechanism, ordered substrate binding where ATP binds first and then streptomycin and diphosphate is released prior to formation of AMP-streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: bifunctional enzyme, adenylation of aminoglycoside antibiotics takes place at the ANT(3'')-Ii domain, aceylation of aminoglycoside antibiotics takes place at the AAC(6')-domain
Products: -
Products: -
?
ATP + streptomycin
diphosphate + adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
-
Substrates: -
Products: -
Products: -
?
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
-
Substrates: -
Products: -
Products: -
?
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not adenylate spectinomycin, enzyme might be identical to AAD aminoglycoside 3''-adenylyltransferase
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not adenylate spectinomycin, enzyme might be identical to AAD aminoglycoside 3''-adenylyltransferase
Products: -
Products: -
?
additional information
?
-
Substrates: no resistance to ampicillin, chloramphenicol, ciprofloxacin, gentamicin, imipenem, penicillin, quinupristin/dalfopristin, rifampin, teicoplanin, and vancomycin mediated
Products: -
Products: -
?
additional information
?
-
-
Substrates: ADP, AMP, UTP, GTP, CTP, TTP, dAMP, adenine, adenosine, S-adenosyl methionine, dADP and ADPglucose are ineffective, streptidine cannot be adenylated by the enzyme, kanamycin and neomycin are not adenylated
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: kanamycin A, gentamycin, and amikacin
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: kanamycin A, gentamycin, and amikacin
Products: -
Products: -
?
additional information
?
-
-
Substrates: adenyltransferase domain is highly specific for spectinomycin and streptomycin and catalyzes the reaction by a Theorell-Chance kinetic mechanism, where ATP binds to the enzyme prior to the aminoglycoside and the modified antibiotic is the last product to be released
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
Acinetobacter sp. NIPH 758 (IIb)
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Acinetobacter sp. NIPH 758 (IIb)
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: enzyme leads to resistance, destroys the inhibitory activity of streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: enzyme leads to resistance, destroys the inhibitory activity of streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: enzyme leads to resistance, destroys the inhibitory activity of streptomycin
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: important mechanism of streptomycin modification is through ATP-dependent O -adenylation
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ADP, AMP, adenosine, adenine other nucleoside triphosphates or other deoxyadenine-containing compounds cannot replace ATP
-
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
Mg2+
additional information
-
Ni2+, Co2+, Ca2+, Zn2+ and Mn2+ cannot replace Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,4R)-4-[3-[(5)-([4-[amino(iminimyl)methyl]phenyl]amino)(carboxylato)methyl]-5-ethoxylphenoxy]-1-methypiperidin-1-ium
-
-
-
(1S,3S,4R)-4-[2-(2-chlorophenoxy)-5,7-dihydroxy-4-oxo-4H-chromen-8-yl]-3-hydroxy-1-methylpiperidin-1-ium
-
-
-
2-(1-(2-(4-methylpiperazin-1-yl)acetyl)-3-oxopiperazin-2-yl)-N-phenylacetamide
-
-
-
2-[[4-[[(4R)-3[(3R)-3-azaniumyl]-4-(2-fluorophenyl)butanoyl]-(1,3-thiazolidin-4-yl]formamido]methyl)phenyl]acetate
-
-
-
9-O-(adenosine-5'-phophoryl)spectinomycin
-
product inhibition of ANT(3'')-Ii domain
clindamycin
residues Phe34, Asp60, Arg63, Gln64, Leu68, Glu87, Thr89, Val90 are responsible for positioning clindamycin into the active site
N-(4-fluorophenyl)-2-(1-(2-(4-methylpiperazin-1-yl)acetyl)-3-oxopiperazin-2-yl)acetamide
-
-
-
tobramycin
-
non-competitive versus streptomycin and uncompetitive versus ATP
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
Pneumonia
Isolation and characterization of the aadA aminoglycoside-resistance gene from Salmonella choleraesuis.
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
0.0014
spectinomycin
-
kinetic parameter of the ANT(3'')-Ii domain of the enzyme
0.0013
streptomycin
-
kinetic parameter of the ANT(3'')-Ii domain of the enzyme
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.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.076
9-O-(adenosine-5'-phophoryl)spectinomycin
-
Kii = 0.089, product inhibition of ANT(3'')-Ii domain, substrate 0.02 mM spectinomycin, noncompetitive/mixed inhibition
0.093
9-O-(adenosine-5'-phophoryl)spectinomycin
-
product inhibition of ANT(3'')-Ii domain, substrate 0.1 mM ATP, competitive inhibition
0.017
AMP-CPP
-
dead-end inhibition of ANT(3'')-Ii domain, substrate 0.1 mM ATP, competitive inhibition
0.021
AMP-CPP
-
dead-end inhibition of ANT(3'')-Ii domain, substrate 0.02 mM spectinomycin, Kii = 0.031 mM, noncompetitive/mixed inhibition
0.004
kanamycin A
-
dead-end inhibition of ANT(3'')-Ii domain, substrate 0.02 mM spectinomycin, competitive inhibition
0.01
kanamycin A
-
Kii = 0.01 mM, dead-end inhibition of ANT(3'')-Ii domain, substrate 0.1 mM ATP, uncompetitive inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE