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Information on EC 6.3.2.64 - bisucaberin synthase
for references in articles please use BRENDA:EC6.3.2.64
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.2 Acid—amino-acid ligases (peptide synthases)
6.3.2.64 bisucaberin synthase
IUBMB Comments
Requires Mg2+. The enzyme, characterized from the bacterium Aliivibrio salmonicida, catalyses the last step in the biosynthesis of the siderophore bisucaberin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylcadaverine, followed by cyclization.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show2
+
2
=
2
+
2
+
Synonyms
avaroferrin siderophore biosynthesis protein, avbD, bibC, BibC C-terminal domain, BibC multienzyme, bisucaberin synthase, desD, IucC-like synthetase, IucC-like type C NIS synthetase, More, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bibC
BibC C-terminal domain
-
-
-
-
bisucaberin synthase
IucC-like synthetase
non-ribosomal peptide synthetase-independent siderophore synthetase
-
pubC
additional information
pubC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine = 2 AMP + 2 diphosphate + bisucaberin
overall reaction
-
-
-
ATP + 2 N1-hydroxy-N1-succinylcadaverine = AMP + diphosphate + bisucaberin B
(1a)
-
-
-
ATP + bisucaberin B = AMP + diphosphate + bisucaberin
(1b)
-
-
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SYSTEMATIC NAME
IUBMB Comments
N1-hydroxy-N1-succinylcadaverine:N1-hydroxy-N1-succinylcadaverine ligase
Requires Mg2+. The enzyme, characterized from the bacterium Aliivibrio salmonicida, catalyses the last step in the biosynthesis of the siderophore bisucaberin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylcadaverine, followed by cyclization.
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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
2 ATP + 3 N-hydroxy-N-succinylcadaverine
2 AMP + 2 diphosphate + desferrioxamine G1
-
Substrates: -
Products: -
Products: -
?
2 ATP + HS[6]A + HS[6]A
2 AMP + 2 diphosphate + macrocycle [6+6]
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + N1-hydroxy-N1-succinylcadaverine + HS[6]A
2 AMP + 2 diphosphate + macrocycle [5+6]
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + N1-hydroxy-N1-succinylcadaverine + N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + avaroferrin
Substrates: overall reaction
Products: -
Products: -
?
ATP + desferrioxamine G1
AMP + diphosphate + desferrioxamine E
-
Substrates: -
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine
2 AMP + 2 diphosphate + bisucaberin
-
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine
2 AMP + 2 diphosphate + bisucaberin
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine
2 AMP + 2 diphosphate + bisucaberin
Shewanella algae B516
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme performs ATP-dependent dimerisation and macrocyclisation of N-hydroxy-N-succinylcadaverine to form bisucaberin
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme performs ATP-dependent dimerisation and macrocyclisation of N-hydroxy-N-succinylcadaverine to form bisucaberin. Desferrioxamine G1 is assembled by ATP-dependent trimerization of N-hydroxy-N-succinylcadaverine (HSC) and it is converted to desferrioxamine E by ATP-dependent macrocyclization. These reactions are catalyzed by DesD, which is the first biochemically characterized member of a putative family of oligomerizing-macrocyclizing enzymes that forms a subset of the type C NIS sythetases
Products: -
Products: -
-
additional information
?
-
-
Substrates: relaxed substrate specificity by synthetic precursors generated 15 different ring-size engineered macrocycles ranging from 18- to 28-membered rings, indicating unprecedented biosynthetic flexibility of the enzyme. The reactions proceed via dimerization and macrocyclization reaction steps. Substrate availability, rather than specificity, of the synthetase determines the production of the corresponding native siderophores by the IucC-like enzymes. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. Chelation of other ions, including Ga3+, vanadate, and molybdate with formation of 1:1 complexes with the majority of macrocycles is determined
Products: -
Products: -
-
additional information
?
-
Substrates: relaxed substrate specificity by synthetic precursors generated 15 different ring-size engineered macrocycles ranging from 18- to 28-membered rings, indicating unprecedented biosynthetic flexibility of the enzyme. The reactions proceed via dimerization and macrocyclization reaction steps. Substrate availability, rather than specificity, of the synthetase determines the production of the corresponding native siderophores by the IucC-like enzymes. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. Chelation of other ions, including Ga3+, vanadate, and molybdate with formation of 1:1 complexes with the majority of macrocycles is determined
Products: -
Products: -
-
additional information
?
-
Substrates: relaxed substrate specificity by synthetic precursors generated 15 different ring-size engineered macrocycles ranging from 18- to 28-membered rings, indicating unprecedented biosynthetic flexibility of the enzyme. The reactions proceed via dimerization and macrocyclization reaction steps. Substrate availability, rather than specificity, of the synthetase determines the production of the corresponding native siderophores by the IucC-like enzymes. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. Chelation of other ions, including Ga3+, vanadate, and molybdate with formation of 1:1 complexes with the majority of macrocycles is determined
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
2 ATP + 3 N-hydroxy-N-succinylcadaverine
2 AMP + 2 diphosphate + desferrioxamine G1
-
Substrates: -
Products: -
Products: -
?
2 ATP + HS[6]A + HS[6]A
2 AMP + 2 diphosphate + macrocycle [6+6]
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + N1-hydroxy-N1-succinylcadaverine + HS[6]A
2 AMP + 2 diphosphate + macrocycle [5+6]
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + N1-hydroxy-N1-succinylcadaverine + N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + avaroferrin
Substrates: overall reaction
Products: -
Products: -
?
ATP + desferrioxamine G1
AMP + diphosphate + desferrioxamine E
-
Substrates: -
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine
2 AMP + 2 diphosphate + bisucaberin
-
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine
2 AMP + 2 diphosphate + bisucaberin
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine
2 AMP + 2 diphosphate + bisucaberin
Shewanella algae B516
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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pH OPTIMUM
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
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
evolution
metabolism
physiological function
evolution
AvbD is more closely related to BibCC, compared to PubC homologues, phylogenetic tree, overview
evolution
-
organization of the bib-bit and des gene clusters, encoding Bib and Des proteins involved in bisucaberin/desferrioxamine biosynthesis, overview. The DesD enzyme and the BibCC domain share 66% sequence similarity
evolution
Shewanella algae B516
-
AvbD is more closely related to BibCC, compared to PubC homologues, phylogenetic tree, overview
-
metabolism
pure putrebactin producers lack the AvbA/BibA homologue of a lysine decarboxylase for cadaverine production and strains producing mainly bisucaberin supposedly have a bias toward generating the cadaverine-derived precursor
metabolism
-
bisucaberin and desferrioxamine G1 both consist of alternating succinic acid and N-hydroxycadaverine units linked by amide bonds. However, bisucaberin contains two molecules each of succinic acid and N-hydroxycadaverine, whereas desferrioxamine G1 contains three molecules of each of these units. The enzyme is involved in the NRPS-independent siderophore (NIS) biosynthetic pathways via the common intermediate HSC. NIS pathways are responsible for the biosynthesis of a wide variety of structurally diverse iron-chelating natural products
metabolism
-
bisucaberin and desferrioxamine G1 both consist of alternating succinic acid and N-hydroxycadaverine units linked by amide bonds. However, bisucaberin contains two molecules each of succinic acid and N-hydroxycadaverine, whereas desferrioxamine G1 contains three molecules of each of these units. The enzyme is involved in the NRPS-independent siderophore (NIS) biosynthetic pathways via the common intermediate N-hydroxy-N-succinylcadaverine (HSC). NIS pathways are responsible for the biosynthesis of a wide variety of structurally diverse iron-chelating natural products
physiological function
bacteria compete for ferric iron by producing siderophores, and some microbes engage in piracy by scavenging siderophores of their competitors. The macrocyclic hydroxamate siderophore avaroferrin of Shewanella algae inhibits swarming of Vibrio alginolyticus by evading this piracy. Avaroferrin, as well as related putrebactin and bisucaberin, are produced by the IucC-like synthetases AvbD, PubC, and BibC. They are capable of synthesizing not only their native product but also other siderophores. Two of the siderophores are obtained in larger quantities by precursor-directed biosynthesis in Shewanella algae, both inhibit swarming motility of Vibrio and, similar to avaroferrin, the most active one exhibits a heterodimeric architecture. AvbD, which is a IucC-like type C NIS synthetase, is responsible for the dimerization and macrocyclization of the monomeric precursors. AvbD shows a much higher affinity and catalytic efficiency for the larger cadaverine-derived substrate HS[5]A, leading to bisucaberin, in comparison to the shorter putrescine-derived HS[4]A, which is the precursor of homodimeric putrebactin. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. None of the compounds has antibacterial activities and also does not inhibit Escherichia coli and Bacillus subtilis up to 0.2 mM
physiological function
bacteria compete for ferric iron by producing siderophores, and some microbes engage in piracy by scavenging siderophores of their competitors. The macrocyclic hydroxamate siderophore avaroferrin of Shewanella algae inhibits swarming of Vibrio alginolyticus by evading this piracy. Avaroferrin, as well as related putrebactin and bisucaberin, are produced by the IucC-like synthetases AvbD, PubC, and BibC. They are capable of synthesizing not only their native product but also other siderophores. Two of the siderophores are obtained in larger quantities by precursor-directed biosynthesis in Shewanella algae, both inhibit swarming motility of Vibrio and, similar to avaroferrin, the most active one exhibits a heterodimeric architecture. None of the compounds has antibacterial activities and also does not inhibit Escherichia coli and Bacillus subtilis up to 0.2 mM
physiological function
bacteria compete for ferric iron by producing siderophores, and some microbes engage in piracy by scavenging siderophores of their competitors. The macrocyclic hydroxamate siderophore avaroferrin of Shewanella algae inhibits swarming of Vibrio alginolyticus by evading this piracy. Avaroferrin, as well as related putrebactin and bisucaberin, are produced by the IucC-like synthetases AvbD, PubC, and BibC. They are capable of synthesizing not only their native product but also other siderophores. Two of the siderophores are obtained in larger quantities by precursor-directed biosynthesis in Shewanella algae, both inhibit swarming motility of Vibrio and, similar to avaroferrin, the most active one exhibits a heterodimeric architecture. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. None of the compounds has antibacterial activities and also does not inhibit Escherichia coli and Bacillus subtilis up to 0.2 mM
physiological function
-
the bisucaberin biosynthetic gene cluster identified in Vibrio salmonicida encodes a domain from within the BibC multienzyme that catalyses ATP-dependent dimerisation and macrocyclisation of N-hydroxy-N-succinylcadaverine to form bisucaberin. BibC is a multienzyme that catalyzes the formation of N1-hydroxy-N1-succinylcadaverine (HSC), followed by its dimerization and subsequent macrocyclization to form bisucaberin
physiological function
Shewanella algae B516
-
bacteria compete for ferric iron by producing siderophores, and some microbes engage in piracy by scavenging siderophores of their competitors. The macrocyclic hydroxamate siderophore avaroferrin of Shewanella algae inhibits swarming of Vibrio alginolyticus by evading this piracy. Avaroferrin, as well as related putrebactin and bisucaberin, are produced by the IucC-like synthetases AvbD, PubC, and BibC. They are capable of synthesizing not only their native product but also other siderophores. Two of the siderophores are obtained in larger quantities by precursor-directed biosynthesis in Shewanella algae, both inhibit swarming motility of Vibrio and, similar to avaroferrin, the most active one exhibits a heterodimeric architecture. AvbD, which is a IucC-like type C NIS synthetase, is responsible for the dimerization and macrocyclization of the monomeric precursors. AvbD shows a much higher affinity and catalytic efficiency for the larger cadaverine-derived substrate HS[5]A, leading to bisucaberin, in comparison to the shorter putrescine-derived HS[4]A, which is the precursor of homodimeric putrebactin. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. None of the compounds has antibacterial activities and also does not inhibit Escherichia coli and Bacillus subtilis up to 0.2 mM
-
physiological function
Shewanella algae B516
-
bacteria compete for ferric iron by producing siderophores, and some microbes engage in piracy by scavenging siderophores of their competitors. The macrocyclic hydroxamate siderophore avaroferrin of Shewanella algae inhibits swarming of Vibrio alginolyticus by evading this piracy. Avaroferrin, as well as related putrebactin and bisucaberin, are produced by the IucC-like synthetases AvbD, PubC, and BibC. They are capable of synthesizing not only their native product but also other siderophores. Two of the siderophores are obtained in larger quantities by precursor-directed biosynthesis in Shewanella algae, both inhibit swarming motility of Vibrio and, similar to avaroferrin, the most active one exhibits a heterodimeric architecture. None of the compounds has antibacterial activities and also does not inhibit Escherichia coli and Bacillus subtilis up to 0.2 mM
-
physiological function
Shewanella algae B516
-
bacteria compete for ferric iron by producing siderophores, and some microbes engage in piracy by scavenging siderophores of their competitors. The macrocyclic hydroxamate siderophore avaroferrin of Shewanella algae inhibits swarming of Vibrio alginolyticus by evading this piracy. Avaroferrin, as well as related putrebactin and bisucaberin, are produced by the IucC-like synthetases AvbD, PubC, and BibC. They are capable of synthesizing not only their native product but also other siderophores. Two of the siderophores are obtained in larger quantities by precursor-directed biosynthesis in Shewanella algae, both inhibit swarming motility of Vibrio and, similar to avaroferrin, the most active one exhibits a heterodimeric architecture. Precursor molecules HS[3]A to HS[6]A, and HS[8]A with different chain lengths in the diamine subunit, are synthesized. The synthetic and native precursors are converted with AvbD, PubC, and BibCC in an ATP reaction buffer. All three enzymes are able to convert the artificial precursors alone or in combination with the native substrates to the corresponding homodimeric and heterodimeric macrocycles. For almost all artificial macrocycles produced, with the exception of [3+3] and [8+3], the corresponding 1:1 iron-siderophore complexes [M+Fe]+ with their characteristic isotopic pattern are detected, indicating the formation of a tetradentate iron chelate. None of the compounds has antibacterial activities and also does not inhibit Escherichia coli and Bacillus subtilis up to 0.2 mM
-
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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). BIBC_ALISL
Aliivibrio salmonicida (strain LFI1238)
819
0
94225
Swiss-Prot
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21star(DE3) by nickel affinity chromatography and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene avbD, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli
gene bibC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli
gene bibC, genetic organization in the bibABCDE gene cluster encoding enzyme for the bisucaberin biosynthesis, DNA and amino acid sequence determination and analysis, recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21star(DE3)
-
gene desD, recombinant His6-tagged enzyme from Escherichia coli strain BL21star(DE3) by nickel affinity chromatography and gel filtration
-
gene pubC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ruetschlin, S.; Gunesch, S.; Boettcher, T.
One enzyme to build them all ring-size engineered siderophores inhibit the swarming motility of Vibrio
ACS Chem. Biol.
13
1153-1158
2018
Shewanella algae, Shewanella algae (A0A1S6Q8L0), Shewanella algae (A0AAD1K9Y4), Shewanella algae B516 (A0A1S6Q8L0), Shewanella algae B516 (A0AAD1K9Y4), Shewanella algae B516
brenda
Kadi, N.; Song, L.; Challis, G.
Bisucaberin biosynthesis an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine
Chem. Commun. (Camb.)
2008
5119-5121
2008
Aliivibrio salmonicida
brenda
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