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Information on EC 3.2.2.26 - futalosine hydrolase
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3.2.2.26 futalosine hydrolaseIUBMB Comments
This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ttha0556, futalosine hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-methylthioadenosine nucleosidase
futalosine hydrolase
-
-
-
-
futalosine nucleosidase
MqnB
MTAN
futalosine nucleosidase
-
-
-
-
MqnB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
futalosine + H2O = dehypoxanthine futalosine + hypoxanthine
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
futalosine ribohydrolase
This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
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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
additional information
?
-
-
no activity with aminodeoxyfutalosine
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
-
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
-
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
-
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
-
-
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
-
-
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
-
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
-
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
-
TTHA0556 is absolutely specific for futalosine and shows no no activity with diverse other structurally related nucleotides and nucleosides, overview
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
S-5'-adenosyl-L-homocysteine + H2O
?
-
-
-
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme activity is not affected by 1 mM of EDTA, Pb2+, Fe2+, Mg2+, Ba2+, Co2+, Zn2+, Ca2+, Ni2+, Cu2+, and Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
-
(2R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(pyrazin-2-yl)sulfanyl]propan-1-ol
-
(2S)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]octan-1-ol
-
(2S,3S,4R,5S)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]pyrrolidine-3,4-diol
-
(2S,3S,4R,5S)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[[(4-chlorophenyl)sulfanyl]methyl]pyrrolidine-3,4-diol
-
(2S,3S,4R,5S)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[[(naphthalen-1-yl)sulfanyl]methyl]pyrrolidine-3,4-diol
-
(3R,4R)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-(hydroxymethyl)pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-(adamant-1-yl)sulfanyl]methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-([[2-(2-hydroxyethoxy)ethyl]sulfanyl]methyl)pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-butylpyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-ethylpyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-methylpyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-propylpyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(butylsulfanyl)methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(cyclohexylsulfanyl)methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(hexylsulfanyl)methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(methylsulfanyl)methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(phenylsulfanyl)methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[2-(hexylsulfanyl)ethyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[2-[2-(2-hydroxyethoxy)ethoxy]ethyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(4-chlorophenyl)sulfanyl]methyl]pyrrolidin-3-ol
-
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(pyrazin-2-yl)sulfanyl]methyl]pyrrolidin-3-ol
-
(3S,4R,5R)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
(3S,4R,5R)-2-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
3-(3-[(3S,4R)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl]propanoyl)benzoic acid
-
3-[3-[(2R,3R,4S,5S)-5-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-3,4-dihydroxypyrrolidin-2-yl]propanoyl]benzoic acid
-
7-(5-S-methyl-5-thio-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
[(3S,4R)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl]methionine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0122
S-5'-adenosyl-L-homocysteine
at pH 7.4 and 25°C
0.0035
6-amino-6-deoxyfutalosine
at pH 7.4 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
S-5'-adenosyl-L-homocysteine
at pH 7.4 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000216
(2R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
at pH 7.4 and 25°C
0.000946
(2R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(pyrazin-2-yl)sulfanyl]propan-1-ol
at pH 7.4 and 25°C
0.0000062
(2S)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]octan-1-ol
at pH 7.4 and 25°C
0.000014
(2S,3S,4R,5S)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]pyrrolidine-3,4-diol
at pH 7.4 and 25°C
0.000028
(2S,3S,4R,5S)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[[(4-chlorophenyl)sulfanyl]methyl]pyrrolidine-3,4-diol
at pH 7.4 and 25°C
0.000422
(2S,3S,4R,5S)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[[(naphthalen-1-yl)sulfanyl]methyl]pyrrolidine-3,4-diol
at pH 7.4 and 25°C
0.0026
(3R,4R)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-(hydroxymethyl)pyrrolidin-3-ol
at pH 7.4 and 25°C
0.000019
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-(adamant-1-yl)sulfanyl]methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000032
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-([[2-(2-hydroxyethoxy)ethyl]sulfanyl]methyl)pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000014
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-butylpyrrolidin-3-ol
at pH 7.4 and 25°C
0.00001
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-ethylpyrrolidin-3-ol
at pH 7.4 and 25°C
0.000055
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-methylpyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000029
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-propylpyrrolidin-3-ol
at pH 7.4 and 25°C
0.00000075
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(butylsulfanyl)methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000022
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(cyclohexylsulfanyl)methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.00000065
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(hexylsulfanyl)methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000029
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(methylsulfanyl)methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.000004
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(phenylsulfanyl)methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.000002
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[2-(hexylsulfanyl)ethyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0017
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[2-[2-(2-hydroxyethoxy)ethoxy]ethyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000031
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(4-chlorophenyl)sulfanyl]methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.0000014
(3R,4S)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(pyrazin-2-yl)sulfanyl]methyl]pyrrolidin-3-ol
at pH 7.4 and 25°C
0.014
(3S,4R,5R)-2-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-5-(hydroxymethyl)pyrrolidine-3,4-diol
at pH 7.4 and 25°C
0.013
(3S,4R,5R)-2-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
at pH 7.4 and 25°C
0.000106
3-(3-[(3S,4R)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl]propanoyl)benzoic acid
at pH 7.4 and 25°C
0.0027
3-[3-[(2R,3R,4S,5S)-5-(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)-3,4-dihydroxypyrrolidin-2-yl]propanoyl]benzoic acid
at pH 7.4 and 25°C
0.022
7-(5-S-methyl-5-thio-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
at pH 7.4 and 25°C
0.000024
[(3S,4R)-1-[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl]methionine
at pH 7.4 and 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
recombinant MBP-fusion and detagged enzymes show similar activities
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme catalyzes the second step of the futalosine pathway starting from chorismate, alternative to the menaquinone pathway, overview
Show AA Sequence and Transmembrane Helices (3059 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23800
-
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
66300
-
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
-
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme or in complex with inhibitors, sitting drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
strain lacking the activity accumulates futalosine. Recombinant expression does not result in an active enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography and cleavage of the tag by Factor Xa
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression of maltose-binding protein fusion enzyme in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
MqnB in Helicobacter pylori is an attractive target for the development of specific anti-Helicobacter pylori drugs
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiratsuka, T.; Furihata, K.; Ishikawa, J.; Yamashita, H.; Itoh, N.; Seto, H.; Dairi, T.
An alternative menaquinone biosynthetic pathway operating in microorganisms
Science
321
1670-1673
2008
Thermus thermophilus (Q5SKT7), Streptomyces coelicolor (Q9KXN0), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SKT7)
brenda
Hiratsuka, T.; Itoh, N.; Seto, H.; Dairi, T.
Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway
Biosci. Biotechnol. Biochem.
73
1137-1141
2009
Thermus thermophilus
brenda
Arakawa, C.; Kuratsu, M.; Furihata, K.; Hiratsuka, T.; Itoh, N.; Seto, H.; Dairi, T.
Diversity of the early step of the futalosine pathway
Antimicrob. Agents Chemother.
55
913-916
2011
Helicobacter pylori, Streptomyces coelicolor, Acidothermus cellulolyticus
brenda
Li, X.; Apel, D.; Gaynor, E.C.; Tanner, M.E.
5'-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni
J. Biol. Chem.
286
19392-19398
2011
Campylobacter jejuni, Thermus thermophilus (Q5SKT7), Streptomyces coelicolor (Q9KXN0), Campylobacter jejuni NCTC 11168
brenda
Kim, R.Q.; Offen, W.A.; Davies, G.J.; Stubbs, K.A.
Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway
Acta Crystallogr. Sect. D
70
177-185
2014
no activity in Helicobacter pylori strain 26695
brenda
Goble, A.M.; Toro, R.; Li, X.; Ornelas, A.; Fan, H.; Eswaramoorthy, S.; Patskovsky, Y.; Hillerich, B.; Seidel, R.; Sali, A.; Shoichet, B.K.; Almo, S.C.; Swaminathan, S.; Tanner, M.E.; Raushel, F.M.
Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes
Biochemistry
52
6525-6536
2013
no activity in Campylobacter jejuni
brenda
Barta, M.L.; Thomas, K.; Yuan, H.; Lovell, S.; Battaile, K.P.; Schramm, V.L.; Hefty, P.S.
Structural and biochemical characterization of Chlamydia trachomatis hypothetical protein CT263 supports that menaquinone synthesis occurs through the futalosine pathway
J. Biol. Chem.
289
32214-32229
2014
no activity in Chlamydia trachomatis
brenda
Ducati, R.G.; Harijan, R.K.; Cameron, S.A.; Tyler, P.C.; Evans, G.B.; Schramm, V.L.
Transition-state analogues of Campylobacter jejuni 5'-methylthioadenosine nucleosidase
ACS Chem. Biol.
13
3173-3183
2018
Campylobacter jejuni subsp. jejuni (Q0PC20), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0PC20)
brenda
Joshi, S.; Fedoseyenko, D.; Mahanta, N.; Manion, H.; Naseem, S.; Dairi, T.; Begley, T.
Novel enzymology in futalosine-dependent menaquinone biosynthesis
Curr. Opin. Chem. Biol.
47
134-141
2018
Streptomyces coelicolor
brenda
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Release 2023.1 (January 2023)
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