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2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
?
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide
-
-
-
?
L-Ala-L-Pro-L-Ala
L-Ala + L-Pro-L-Ala
-
-
-
?
L-Ala-L-Pro-L-Ala + H2O
L-Ala + L-Pro-L-Ala
-
-
-
?
L-Val-L-Pro-L-Leu + H2O
L-Val + L-Pro-L-Leu
-
-
-
?
(2-aminobenzoyl)-Lys-Pro-Pro-4-nitroanilide + H2O
?
-
-
-
-
?
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
-
?
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O
(4-nitro)Phe + Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
-
?
Abz-L-Lys-L-Pro-L-Pro-p-nitroanilide + H2O
Abz-L-Lys + L-Pro-L-Pro-p-nitroanilide
-
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
-
?
Ala-Pro-p-nitroanilide + H2O
Ala + Pro-p-nitroanilide
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
i.e. bradykinin
one Arg is released per mol of bradykinin in less than 5 min, the following Pro residue is released within 1 h
?
bradykinin + H2O
des-Arg-bradykinin + L-Arg
-
-
-
-
?
centrosomal protein 290 kDa/NPHP6 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
Glu-Pro-p-nitroanilide + H2O
Glu + Pro-p-nitroanilide
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro-2-naphthylamide + H2O
Gly + Pro-2-naphthylamide
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly + Pro-4-methylcoumarin 7-amide
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
?
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly + Pro-p-nitroanilide
-
-
-
-
?
His-Pro-p-nitroanilide + H2O
His + Pro-p-nitroanilide
-
-
-
-
?
L-Ala-L-Pro-L-Ala + H2O
L-Ala + L-Pro-L-Ala
-
-
-
-
?
L-Asn-L-Pro-L-Thr-L-Asn-L-Leu-L-His + H2O
L-Asn + L-Pro-L-Thr-L-Asn-L-Leu-L-His
-
-
-
-
?
L-Met-L-Ala-L-Ser + H2O
L-Met + L-Ala-L-Ser
-
-
-
-
?
L-Met-L-Pro-Gly + H2O
L-Met + L-Pro-Gly
-
-
-
-
?
L-Met-L-Ser-Gly + H2O
L-Met + L-Ser-Gly
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
leucine rich repeat containing 50 + H2O
?
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys + Pro-p-nitroanilide
-
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
papain + H2O
?
-
reduced and carboxymethylated, with the N-terminal sequence Ile-Pro-Glu-Tyr-Val
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
-
?
Pro-Pro + H2O
Pro
-
-
-
-
?
Pro-Pro-Ala + H2O
?
-
-
-
-
?
Pro-Pro-Gly-(Pro-Pro-Gly)4 + H2O
?
-
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser + Pro-p-nitroanilide
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
-
?
additional information
?
-
Met-Pro + H2O
Met + Pro
-
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
additional information
?
-
peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates
-
-
?
additional information
?
-
-
peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates
-
-
?
additional information
?
-
-
the enzyme can only hydrolyze the trans form of the X-L-Pro-peptide bond, the cis form has to isomerize before it can be cleaved
-
-
?
additional information
?
-
-
enzyme hydrolyzes the Xaa-Pro peptide bond when the first amino acid is Asn, Ala, or Met
-
-
?
additional information
?
-
-
ciliary proteome is screened for proteins with a proline in the second position: 3 candidate substrates centrosomal protein 290 kDa/NPHP6 (CEP290/NPHP6), Alstrom syndrome 1 (ALMS1), and leucine rich repeat containing 50 (LRRC50), known to cause cystic renal disease are shown to be cleaved by ecAPP
-
-
?
additional information
?
-
substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ni2+
-
may substitute for Co2+
Zn2+
required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA is coordinated by O1 of cacodylate ion, Glu335 Oepsilon2, Glu321 Oepsilon2, His292 Nepsilon2, and Asp223 Odelta2. Metal ZnB is coordinated by O1 of cacodylate ion, Glu335 Oepsilon1, Asp212 Odelta1, and Asp223 Odelta1. Glu335 and Asp223 act as bidentate ligands and bind to both the metals
Mn2+
required
Mn2+
2 mol of Mn2+ ions per mol of enzyme
Co2+
-
required
Mn2+
required
Mn2+
-
activates, sharp optimum at 0.37 mM
Mn2+
-
0.05 mM, 3-4fold activatiion
Mn2+
-
0.005 mM, 3fold activation
Mn2+
-
2 ions per enzyme molecule, ligand binding structure determination
Mn2+
-
may substitute for Co2+
Mn2+
-
wild-type and mutat R404A, binding of Mn2+ with a stoichiometry of 2 per monomer
additional information
not activating: Mg2+, Zn2+, Na+, Ca2+
additional information
-
not activating: Mg2+, Zn2+, Na+, Ca2+
additional information
-
the active site contains a dinuclear metal binding site, the enzyme contains 12 metal atoms per molecule, 2 of which are Mn2+ ions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-Ala-(N-methyl)L-Ala-L-Ala
competitive
L-Ala-L-Ala-L-Ala
competitive
L-Pro-L-Leu
product inhibition, a third metal binding site is formed by two conserved His-residues and L-Pro-L-Leu
(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
-
-
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
-
-
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
-
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
-
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
slow-binding inhibitors
-
acetyl-Phe(NO2)-Pro-Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
0.5 mM, 30% inhibition of hydrolysis of (4-nitr)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
apstatin
-
binds to the active site with its N-terminal amino group coordinated to one of the two Mn(II) ions at the metal center
Peptides with N-terminal Pro
-
product inhibition
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
0.01 mM, complete inhibition of hydrolysis of (4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-2-aminobenzoyl
L-Ala-L-Pro-L-Ala
competitive
L-Ala-L-Pro-L-Ala
competitive, 50% inhibition at 0.22 mM
EDTA
-
-
EDTA
-
0.1-1 mM, completely
EDTA
-
reactivation by Mn2+, Co2+, Cd2+, or Ni2+
additional information
not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala
-
additional information
-
not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.087 - 0.14
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide
0.087 - 0.14
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
0.77
L-Ala-L-Pro-L-Ala
wild-type, pH 8.1, 37°C
3
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
0.22
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
0.23
Met-Ala-Ala
pH 8.0, 55°C, recombinant wild-type
7.9
Met-Pro
pH 8.0, 55°C, recombinant wild-type
3
Met-Pro-Ala
pH 8.0, 55°C, recombinant wild-type
additional information
additional information
-
-
-
0.087
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide
wild-type, pH 8.1, 37°C
0.14
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide
mutant H350A, pH 8.1, 37°C
0.087
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
wild-type, pH 8.1, 37°C
0.14
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
mutant H350, pH 8.1, 37°C
0.047
bradykinin
-
mutant R404A, pH 7.5, 37°C
0.16
bradykinin
-
mutant R153W/R370L, pH 7.5, 37°C
0.18
bradykinin
-
mutant R153L/R370L, pH 7.5, 37°C
0.21
bradykinin
-
mutant R370L, pH 7.5, 37°C
0.41
bradykinin
-
mutant R404K, pH 7.5, 37°C
0.42
bradykinin
-
mutant R153A, pH 7.5, 37°C
0.43
bradykinin
-
mutant R153W, pH 7.5, 37°C
0.51
bradykinin
-
mutant R153L, pH 7.5, 37°C
0.78
bradykinin
-
wild-type, pH 7.5, 37°C
0.84
bradykinin
-
mutant Y387F, pH 7.5, 37°C
1.02
bradykinin
-
mutant W88L, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.3 - 95
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
0.77
L-Ala-L-Pro-L-Ala
wild-type, pH 8.1, 37°C
135
(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
20
(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
-
-
1.5
Met-Ala-Ala
pH 8.0, 55°C, recombinant wild-type
33
Met-Pro
pH 8.0, 55°C, recombinant wild-type
2 - 8
Met-Pro-Ala
pH 8.0, 55°C, recombinant wild-type
7.3
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
mutant H350, pH 8.1, 37°C
95
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide
wild-type, pH 8.1, 37°C
0.17
bradykinin
-
mutant R404A, pH 7.5, 37°C
0.24
bradykinin
-
mutant R404K, pH 7.5, 37°C
4.2
bradykinin
-
mutant Y387F, pH 7.5, 37°C
13.8
bradykinin
-
mutant W88L, pH 7.5, 37°C
57
bradykinin
-
mutant R153L/R370L, pH 7.5, 37°C
69
bradykinin
-
wild-type, pH 7.5, 37°C
70
bradykinin
-
mutant R153W, pH 7.5, 37°C
72
bradykinin
-
mutant R153A, pH 7.5, 37°C
87
bradykinin
-
mutant R153W/R370L, pH 7.5, 37°C
102
bradykinin
-
mutant R370L, pH 7.5, 37°C
109
bradykinin
-
mutant R153L, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Mn(II)-form of enzyme and substituted with Mg2+, Zn2+, Ca2+, Na+ and apo-enzyme in complex with L-Val-L-Pro-L-Leu
mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group
mutants H243A, D260A, D271A, H350A, H354A, H361A, E383A
8 mg/ml purified recombinant enzyme in Tris, pH 8.5, hanging drop vapour diffusion method, 0.003 ml mixed with 0.002 ml reservoir solution containing 25% PEG 4000, 0.1 M Tris-HCl, pH 8.0, 0.2 M sodium acetate, and 1 mM MnCl2, 1 month at 4°C, cryoprotectant is 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
in complex with inhibitor apstatin
-
purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml of crystallization solution containing 1.4 M trisodium citrate, 0.1 M sodium cacodylate, pH 6.5, 10% glycerol, and 0.5 mM ZnCl2, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Yoshimoto, T.; Murayama, N.; Tsuru, D.
A novel assay method for aminopeptidase P and partial purification of two types of the enzyme in Escherichia coli
Agric. Biol. Chem.
52
1957-1963
1988
Escherichia coli
-
brenda
Yoshimoto, T.; Murayama, N.; Honda, T.; Tone, H.; Tsuru, D.
Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme
J. Biochem.
104
93-97
1988
Escherichia coli
brenda
Lin, L.N.; Brandts, J.F.
Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease
Biochemistry
19
3055-3059
1980
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Yaron, A.; Berger, A.
Aminopeptidase-P
Methods Enzymol.
19
521-534
1970
Escherichia coli
-
brenda
Yaron, A.; Mlynar, D.
Aminopeptidase-P
Biochem. Biophys. Res. Commun.
32
658-663
1968
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Fleminger, G.; Carmel, A.; Goldenberg, D.; Yaron, A.
Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung
Eur. J. Biochem.
125
609-615
1982
Bos taurus, Escherichia coli, Homo sapiens
brenda
Lin, L.N.; Brandts, J.F.
Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyproline
Biochemistry
18
5037-5042
1979
Escherichia coli
brenda
Stckel, A.; Stiebitz, B.; Neubert, K.
Specific inhibitors of aminopeptidase P. Peptides and pseudopeptides of 2-hydroxy-3-amino acids
Adv. Exp. Med. Biol.
421
31-35
1997
Escherichia coli, Rattus norvegicus
brenda
Graham, S.C.; Lee, M.; Freeman, H.C.; Guss, J.M.
An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution
Acta Crystallogr. Sect. D
59
897-902
2003
Escherichia coli
brenda
Graham, S.C.; Maher, M.J.; Simmons, W.H.; Freeman, H.C.; Guss, J.M.
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin
Acta Crystallogr. Sect. D
D60
1770-1779
2004
Escherichia coli
brenda
Graham, S.C.; Bond, C.S.; Freeman, H.C.; Guss, J.M.
Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center
Biochemistry
44
13820-13836
2005
Escherichia coli (P15034), Escherichia coli
brenda
Jao, S.C.; Huang, L.F.; Hwang, S.M.; Li, W.S.
Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P
Biochemistry
45
1547-1553
2006
Escherichia coli
brenda
Graham, S.C.; Lilley, P.E.; Lee, M.; Schaeffer, P.M.; Kralicek, A.V.; Dixon, N.E.; Guss, J.M.
Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis
Biochemistry
45
964-975
2006
Escherichia coli (P15034), Escherichia coli
brenda
Stockel-Maschek, A.; Stiebitz, B.; Koelsch, R.; Neubert, K.
Novel 3-amino-2-hydroxy acids containing protease inhibitors. Part 1: Synthesis and kinetic characterization as aminopeptidase P inhibitors
Bioorg. Med. Chem.
13
4806-4820
2005
Escherichia coli, Rattus norvegicus
brenda
Zheng, Y.; Roberts, R.J.; Kasif, S.; Guan, C.
Characterization of two new aminopeptidases in Escherichia coli
J. Bacteriol.
187
3671-3677
2005
Escherichia coli
brenda
Graham, S.C.; Guss, J.M.
Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu
Arch. Biochem. Biophys.
469
200-208
2008
Escherichia coli (P15034), Escherichia coli
brenda
OToole, J.F.; Liu, Y.; Davis, E.E.; Westlake, C.J.; Attanasio, M.; Otto, E.A.; Seelow, D.; Nurnberg, G.; Becker, C.; Nuutinen, M.; Kaerppae, M.; Ignatius, J.; Uusimaa, J.; Pakanen, S.; Jaakkola, E.; van den Heuvel, L.P.; Fehrenbach, H.; Wiggins, R.; Goyal, M.; Zhou, W.; Wolf, M.T.; Wise, E.; Helou, J.; A, A.l.
Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy
J. Clin. Invest.
120
791-802
2010
Danio rerio, Escherichia coli, Homo sapiens (Q9NQH7), Homo sapiens
brenda
Are, V.; Kumar, A.; Goyal, V.; Gotad, S.; Ghosh, B.; Gadre, R.; Jamdar, S.; Makde, R.
Structures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidases
Proteins
87
212-225
2018
Deinococcus radiodurans (Q9RUY4), Deinococcus radiodurans ATCC 13939 (Q9RUY4), Deinococcus radiodurans DSM 20539 (Q9RUY4), Deinococcus radiodurans JCM 16871 (Q9RUY4), Deinococcus radiodurans LMG 4051 (Q9RUY4), Deinococcus radiodurans NBRC 15346 (Q9RUY4), Deinococcus radiodurans NCIMB 9279 (Q9RUY4), Deinococcus radiodurans R1 (Q9RUY4), Deinococcus radiodurans VKM B-1422 (Q9RUY4), Escherichia coli (P76524), Mycobacterium tuberculosis (I6YDN6), Mycobacterium tuberculosis ATCC 25618 (I6YDN6), Mycobacterium tuberculosis H37Rv (I6YDN6)
brenda