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Information on EC 4.2.1.143 - versicolorin B synthase
for references in articles please use BRENDA:EC4.2.1.143
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IUBMB Comments
Isolated from the aflatoxin-producing mold Aspergillus parasiticus. Involved in aflatoxin biosynthesis.
The enzyme appears in viruses and cellular organisms
- 4.2.1.143
- aflatoxin
- aspergillus
- hemiacetal
- parasiticus
-
mycotoxin
-
cyclization
-
racemic
- coumarins
-
flavoenzymes
- polyketide
-
adp-binding
showSynonyms
versicolorin b synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aflK
OAVN cyclase
-
-
-
-
VBS
versicolorin B synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
versiconal = versicolorin B + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
versicolorin B biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
versiconal hydro-lyase (versicolorin-B forming)
Isolated from the aflatoxin-producing mold Aspergillus parasiticus. Involved in aflatoxin biosynthesis.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
versiconal
(-)-versicolorin B + H2O
-
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
?
versiconal
(-)-versicolorin B + H2O
-
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
?
versiconal
versicolorin B + H2O
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
Substrates: -
Products: -
Products: -
?
versiconal
versicolorin B + H2O
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
?
versiconal
versicolorin B + H2O
-
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
?
versiconal
versicolorin B + H2O
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione
?
versiconal hemiacetal
versicolorin B + H2O
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione,
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione,
?
versiconal hemiacetal
versicolorin B + H2O
Substrates: i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione,
Products: (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione,
?
additional information
?
-
Substrates: enzyme selects from two equilibrating enantiomers of versiconal hemiacetal to cyclize the appropriate antipode to optically pure versicolorin B. By varying the amount of enzyme to a fixed concentration of substrate, the rate of enzymic cyclization can be limited by the intrinsic rate of enantiomerization of the substrate under the conditions of reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme selects from two equilibrating enantiomers of versiconal hemiacetal to cyclize the appropriate antipode to optically pure versicolorin B. By varying the amount of enzyme to a fixed concentration of substrate, the rate of enzymic cyclization can be limited by the intrinsic rate of enantiomerization of the substrate under the conditions of reaction
Products: -
Products: -
?
additional information
?
-
Substrates: in addition, enzyme catalyzes the conversion of 5'-oxoaverantin to (2'S,5'S)-averufin, reaction of EC 4.2.1.142, 5'-oxoaverantin cyclase
Products: -
Products: -
?
additional information
?
-
-
Substrates: racemic versiconal hemiacetate or racemic versiconal leads exclusively to formation of (1'R,2'S)-(-)-versicolorin B. Only (1'R,2'S)-(-)-versicolorin B, and not (1'S,2'R)-(+)antipode, serves as a substrate for desaturase activity in the following reaction of the aflatoxin biosynthetic pathway. Thus the stereoconfiguration of bis-furan moiety in aflatoxin molecules is determined by the cyclase enzyme catalyzing the reaction from versiconal to versicolorinB. Nonenzymatic racemization in both the (2'R)- and (2'S)-versiconal hemiacetate enantiomers is dependent upon the temperature and alkaline conditions
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme selects from two equilibrating enantiomers of versiconal hemiacetal to cyclize the appropriate antipode to optically pure versicolorin B. By varying the amount of enzyme to a fixed concentration of substrate, the rate of enzymic cyclization can be limited by the intrinsic rate of enantiomerization of the substrate under the conditions of reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: racemic versiconal hemiacetate or racemic versiconal leads exclusively to formation of (1'R,2'S)-(-)-versicolorin B. Only (1'R,2'S)-(-)-versicolorin B, and not (1'S,2'R)-(+)antipode, serves as a substrate for desaturase activity in the following reaction of the aflatoxin biosynthetic pathway. Thus the stereoconfiguration of bis-furan moiety in aflatoxin molecules is determined by the cyclase enzyme catalyzing the reaction from versiconal to versicolorinB. Nonenzymatic racemization in both the (2'R)- and (2'S)-versiconal hemiacetate enantiomers is dependent upon the temperature and alkaline conditions
Products: -
Products: -
?
additional information
?
-
Substrates: in addition, enzyme catalyzes the conversion of 5'-oxoaverantin to (2'S,5'S)-averufin, reaction of EC 4.2.1.142, 5'-oxoaverantin cyclase
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
versiconal
versicolorin B + H2O
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-ethyl-3(3-dimethylaminopropyl)carbodiimide
10 mM, 12% residual activity
3-(2-hydroxyethyl)-2,3-dihydro-1-benzofuran-2,4-diol
competitive
3-(2-hydroxyethyl)-2,3-dihydro-1-benzofuran-2,4-diol
0.05 mM, 30% inhibition. Compound mimics the C-ring and side chain of the substrate
additional information
not inhibitory: FAD, FMN, riboflavin, and glucose
-
additional information
-
not inhibitory: FAD, FMN, riboflavin, and glucose
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.076
3-(2-hydroxyethyl)-2,3-dihydro-1-benzofuran-2,4-diol
pH 6.5, 37Ā°C
0.096
3-(2-hydroxyethyl)-2,3-dihydro-1-benzofuran-2,4-diol
pH 6.5, 37Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest abundance of enzyme in colony fraction S2 consisting of cells that have grown for 24-48 h
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme distributes throughout the cytoplasm and concentrates in ring-like structures surrounding nuclei
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
conidiation phenotype and sclerotial phenotype of wild-type, enzyme deletion DELTAaflK, and complemented mutant DELTA aflK::aflK strains, overview. The aflK deletion-mutant DELTAaflK exhibits a significant decrease in sclerotial production and aflatoxin biosynthesis compared with wild-type and the complementation strain DELTAaflK::aflK. The mutation DELTAaflK does not affect the ability of Aspergillus flavus to infect seeds, but downregulates aflatoxin production after seed infection
malfunction
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
-
conidiation phenotype and sclerotial phenotype of wild-type, enzyme deletion DELTAaflK, and complemented mutant DELTA aflK::aflK strains, overview. The aflK deletion-mutant DELTAaflK exhibits a significant decrease in sclerotial production and aflatoxin biosynthesis compared with wild-type and the complementation strain DELTAaflK::aflK. The mutation DELTAaflK does not affect the ability of Aspergillus flavus to infect seeds, but downregulates aflatoxin production after seed infection
-
metabolism
genes aflD, aflK, aflQ, and aflR are involved in aflatoxin biosynthesis
metabolism
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
-
genes aflD, aflK, aflQ, and aflR are involved in aflatoxin biosynthesis
-
physiological function
enzyme catalyzes bisfuran ring closure in versiconal hemiacetal to form versicolorin B. This reaction is required for the subsequent activation to aflatoxin B1-8,9 epoxide, a highly reactive and toxic aflatoxin metabolite
physiological function
enzyme is involved in aflatoxin biosynthesis. A deletion mutant accumulates large amounts of 5'-oxoaverantin, 5'-hydroxyaverantin, averantin, (2'S,5'S)-averufin, and averufanin in the mycelium, leading to bright orange colour
physiological function
the enzyme is encoded by gene alfK, which is part of the gene cluster involved in aflatoxin biosynthesis. Negative role of aflK in sclerotial production. Relationship between enzyme AflK and sclerotial production in Aspergillus flavus
physiological function
-
enzyme is involved in aflatoxin biosynthesis. A deletion mutant accumulates large amounts of 5'-oxoaverantin, 5'-hydroxyaverantin, averantin, (2'S,5'S)-averufin, and averufanin in the mycelium, leading to bright orange colour
-
physiological function
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
-
the enzyme is encoded by gene alfK, which is part of the gene cluster involved in aflatoxin biosynthesis. Negative role of aflK in sclerotial production. Relationship between enzyme AflK and sclerotial production in Aspergillus flavus
-
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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). STCN_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
639
0
69851
Swiss-Prot
Secretory Pathway (Reliability: 1)
VBSA_DOTSE
647
0
70966
Swiss-Prot
Secretory Pathway (Reliability: 1)
VBSA_DOTSN
Dothistroma septosporum (strain NZE10 / CBS 128990)
647
0
70966
Swiss-Prot
Secretory Pathway (Reliability: 1)
AFLK_ASPPU
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
643
1
70271
Swiss-Prot
Secretory Pathway (Reliability: 1)
B8NHY3_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
643
0
70264
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
x * 78000, SDS-PAGE, recombinant protein, x * 70000, SDS-PAGE of PNGase F treated protein
72000
78000
78000
x * 78000, SDS-PAGE, recombinant protein, x * 70000, SDS-PAGE of PNGase F treated protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
x * 78000, SDS-PAGE, recombinant protein, x * 70000, SDS-PAGE of PNGase F treated protein
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
native enzyme contains three potential sites for N-linked glycosylation
glycoprotein
sequence contains 3 potential N-glycosylation sites. Treatment with PNGase F leads to a decrease in molecular mass from 78000 kDa for wild-type to 70000 kDa
glycoprotein
-
native enzyme contains three potential sites for N-linked glycosylation
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
aflK mutant construction by gene replacement. The aflK deletion-mutant DELTAaflK exhibits a significant decrease in sclerotial production and aflatoxin biosynthesis compared with wild-type and the complementation strain DELTAaflK::aflK. The mutation DELTAaflK does not affect the ability of Aspergillus flavus to infect seeds, but downregulates aflatoxin production after seed infection
additional information
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
-
aflK mutant construction by gene replacement. The aflK deletion-mutant DELTAaflK exhibits a significant decrease in sclerotial production and aflatoxin biosynthesis compared with wild-type and the complementation strain DELTAaflK::aflK. The mutation DELTAaflK does not affect the ability of Aspergillus flavus to infect seeds, but downregulates aflatoxin production after seed infection
-
additional information
truncation of the N-terminal 41-amino-acid region may not affect the substrate specificity
additional information
-
truncation of the N-terminal 41-amino-acid region may not affect the substrate specificity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene alfK, encoded in the gene cluster involved in aflatoxin biosynthesis, sequence comparisons and phylogenetic analysis and tree, RT-PCR enzyme expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
thiabendazole, 4-hydroxy-7-methoxy-3-phenylcoumarin, 4-hydroxy-6,7-dimethylcoumarin, 6,7-dimethoxycoumarin, 4-(bromomethyl)-6,7-dimethoxycoumarin, and 1-(2-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one show potent antifungal and antiaflatoxigenic activities against Aspergillus flavus. Inhibitory mode of antiaflatoxigenic action by 4-hydroxy-7-methyl-3-phenyl coumarin is based on the downregulation of aflD, aflK, aflQ, and aflR in aflatoxin biosynthesis. The inhibitory mode of antiaflatoxigenic action by 2,3-dihydrobenzofuran is based on the inhibition of the transcription factor (aflS) in the aflatoxin biosynthesis pathway. Complete inhibition of growth at 1 mg/ml
thiabendazole, 4-hydroxy-7-methoxy-3-phenylcoumarin, 4-hydroxy-6,7-dimethylcoumarin, 6,7-dimethoxycoumarin, 4-(bromomethyl)-6,7-dimethoxycoumarin, and 1-(2-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one show potent antifungal and antiaflatoxigenic activities against Aspergillus flavus. Inhibitory mode of antiaflatoxigenic action by 4-hydroxy-7-methyl-3-phenyl coumarin is based on the downregulation of aflD, aflK, aflQ, and aflR in aflatoxin biosynthesis. The inhibitory mode of antiaflatoxigenic action by 2,3-dihydrobenzofuran is based on the inhibition of the transcription factor (aflS) in the aflatoxin biosynthesis pathway. Complete inhibition of growth at 1 mg/ml
thiabendazole, 4-hydroxy-7-methoxy-3-phenylcoumarin, 4-hydroxy-6,7-dimethylcoumarin, 6,7-dimethoxycoumarin, 4-(bromomethyl)-6,7-dimethoxycoumarin, and 1-(2-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one show potent antifungal and antiaflatoxigenic activities against Aspergillus flavus. Inhibitory mode of antiaflatoxigenic action by 4-hydroxy-7-methyl-3-phenyl coumarin is based on the downregulation of aflD, aflK, aflQ, and aflR in aflatoxin biosynthesis. The inhibitory mode of antiaflatoxigenic action by 2,3-dihydrobenzofuran is based on the inhibition of the transcription factor (aflS) in the aflatoxin biosynthesis pathway. Complete inhibition of growth at 1 mg/ml
Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yabe, K.; Hamasaki, T.
Stereochemistry during aflatoxin biosynthesis: Cyclase reaction in the conversion of versiconal to versicolorin B and racemization of versiconal hemiacetal acetate
Appl. Environ. Microbiol.
59
2493-2500
1993
Aspergillus parasiticus, Aspergillus parasiticus NIAH-26
brenda
Sakuno, E.; Wen, Y.; Hatabayashi, H.; Arai, H.; Aoki, C.; Yabe, K.; Nakajima, H.
Aspergillus parasiticus cyclase catalyzes two dehydration steps in aflatoxin biosynthesis
Appl. Environ. Microbiol.
71
2999-3006
2005
Aspergillus parasiticus (Q12062), Aspergillus parasiticus NRRL 2999 (Q12062)
brenda
Lin, B.; Anderson, J.
Purification and properties of versiconal cyclase from Aspergillus parasiticus
Arch. Biochem. Biophys.
293
67-70
1992
Aspergillus parasiticus, Aspergillus parasiticus SU-1
brenda
Chiou, C.H.; Lee, L.W.; Owens, S.A.; Whallon, J.H.; Klomparens, K.L.; Townsend, C.A.; Linz, J.E.
Distribution and sub-cellular localization of the aflatoxin enzyme versicolorin B synthase in time-fractionated colonies of Aspergillus parasiticus
Arch. Microbiol.
182
67-79
2004
Aspergillus parasiticus (Q12062), Aspergillus parasiticus
brenda
McGuire, S.M.; Silva, J.C.; Casillas, E.G.; Townsend, C.A.
Purification and characterization of versicolorin B synthase from Aspergillus parasiticus. Catalysis of the stereodifferentiating cyclization in aflatoxin biosynthesis essential to DNA interaction
Biochemistry
35
11470-11486
1996
Aspergillus parasiticus (Q12062), Aspergillus parasiticus, Aspergillus parasiticus ATCC 56775 (Q12062)
brenda
Silva, J.C.; Minto, R.E.; Barry, C.E.; Holland, K.A.; Townsend, C.A.
Isolation and characterization of the versicolorin B synthase gene from Aspergillus parasiticus. Expansion of the aflatoxin b1 biosynthetic gene cluster
J. Biol. Chem.
271
13600-13608
1996
Aspergillus parasiticus (Q12062), Aspergillus parasiticus, Aspergillus parasiticus ATCC 56775 (Q12062)
brenda
Silva, J.C.; Townsend, C.A.
Heterologous expression, isolation, and characterization of versicolorin B synthase from Aspergillus parasiticus. A key enzyme in the aflatoxin B1 biosynthetic pathway
J. Biol. Chem.
272
804-813
1997
Aspergillus parasiticus (Q12062), Aspergillus parasiticus
brenda
Ren, S.; Yue, Y.; Li, Y.; Guo, X.; Wang, S.
Functional analyses of the versicolorin B synthase gene in Aspergillus flavus
MicrobiologyOpen
6
e00471
2017
Aspergillus flavus (B8NHY3), Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167 (B8NHY3)
brenda
Moon, Y.S.; Kim, L.; Chun, H.S.; Lee, S.E.
4-Hydroxy-7-methyl-3-phenylcoumarin suppresses aflatoxin biosynthesis via downregulation of aflk expressing versicolorin B synthase in aspergillus flavus
Molecules
22
712
2017
Aspergillus flavus (B8NHY3), Aspergillus flavus, Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167 (B8NHY3)
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.143)
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