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Information on EC 6.3.2.63 - putrebactin synthase
for references in articles please use BRENDA:EC6.3.2.63
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.2 Acid—amino-acid ligases (peptide synthases)
6.3.2.63 putrebactin synthase
IUBMB Comments
Requires Mg2+. The enzyme, characterized from the bacteria Shewanella spp. MR-4 and MR-7, catalyse the last step in the biosynthesis of the siderophore putrebactin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylputrescine, followed by cyclization.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show2
+
2
=
2
+
2
+
Synonyms
avaroferrin siderophore biosynthesis protein, avbD, bibC, desD, IucC-like synthetase, IucC-like type C NIS synthetase, More, NIS synthetase, non-ribosomal peptide synthetase-independent siderophore synthetase, NTP-dependent putrebactin synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
avaroferrin siderophore biosynthesis protein
avbD
bibC
IucC-like synthetase
IucC-like type C NIS synthetase
non-ribosomal peptide synthetase-independent siderophore synthetase
-
NTP-dependent putrebactin synthetase
pubC
type C NIS sythetase
pubC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ATP + 2 N1-hydroxy-N1-succinylputrescine = 2 AMP + 2 diphosphate + putrebactin
overall reaction
-
-
-
ATP + 2 N1-hydroxy-N1-succinylputrescine = AMP + diphosphate + pre-putrebactin
(1a)
-
-
-
ATP + pre-putrebactin = AMP + diphosphate + putrebactin
(1b)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
N1-hydroxy-N1-succinylputrescine:N1-hydroxy-N1-succinylputrescine ligase
Requires Mg2+. The enzyme, characterized from the bacteria Shewanella spp. MR-4 and MR-7, catalyse the last step in the biosynthesis of the siderophore putrebactin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylputrescine, 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-succinylputrescine + HS[6]A
2 AMP + 2 diphosphate + macrocycle [4+6]
Substrates: overall reaction
Products: -
Products: -
?
ATP + desferrioxamine G1
AMP + diphosphate + desferrioxamine E
-
Substrates: -
Products: -
Products: -
?
2 ATP + 2 HS[5]A
2 AMP + 2 diphosphate + bisucaberin
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 HS[5]A
2 AMP + 2 diphosphate + bisucaberin
Shewanella algae B516
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: putrescine-derived substrate HS[4]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Shewanella algae B516
Substrates: putrescine-derived substrate HS[4]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Shewanella algae MR-4
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Shewanella algae MR-7
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + HS[5]A + N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + avaroferrin
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + HS[5]A + N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + avaroferrin
Shewanella algae B516
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: ATP-dependent head-to-tail dimerization of HSP
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae B516
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae MR-4
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae MR-4
Substrates: ATP-dependent head-to-tail dimerization of HSP
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae MR-7
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae MR-7
Substrates: ATP-dependent head-to-tail dimerization of HSP
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: ATP-dependent head-to-tail dimerization of HSP
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: ATP-dependent head-to-tail dimerization of HSP
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Shewanella algae B516
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Shewanella algae MR-4
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Shewanella algae MR-7
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
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: -
-
additional information
?
-
-
Substrates: desferrioxamine G1 is assembled by ATP-dependent trimerization of N-hydroxy-N-succinylcadaverine (HSC) and 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 form a subset of the type C NIS synthetases
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: -
?
ATP + desferrioxamine G1
AMP + diphosphate + desferrioxamine E
-
Substrates: -
Products: -
Products: -
?
2 ATP + 2 HS[5]A
2 AMP + 2 diphosphate + bisucaberin
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 HS[5]A
2 AMP + 2 diphosphate + bisucaberin
Shewanella algae B516
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: putrescine-derived substrate HS[4]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Shewanella algae B516
Substrates: putrescine-derived substrate HS[4]A, overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Shewanella algae MR-4
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Shewanella algae MR-7
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + 2 N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + putrebactin
Substrates: overall reaction
Products: -
Products: -
?
2 ATP + HS[5]A + N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + avaroferrin
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
2 ATP + HS[5]A + N1-hydroxy-N1-succinylputrescine
2 AMP + 2 diphosphate + avaroferrin
Shewanella algae B516
Substrates: cadaverine-derived substrate HS[5]A, overall reaction
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae B516
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae MR-4
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Shewanella algae MR-7
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + 2 N1-hydroxy-N1-succinylputrescine
AMP + diphosphate + pre-putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Shewanella algae B516
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Shewanella algae MR-4
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Shewanella algae MR-7
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
ATP + pre-putrebactin
AMP + diphosphate + putrebactin
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
pubABC encode the enzymes required to assemble putrebactin from putrescine. PubA catalyzes the O2- and FADH2-dependent hydroxylation of putrescine to give N-hydroxyputrescine. PubB can catalyze succinyl-CoA dependent succinylation of N-hydroxyputrescine to give N-hydroxy-N-succinyl-putrescine (HSP), and PubC can catalyze ATP-dependent head-to-tail dimerization of HSP to give pre-putrebactin and subsequent macrocyclization of pre-putrebactin to give putrescine
metabolism
pubABC encode the enzymes required to assemble putrebactin from putrescine. PubA catalyzes the O2- and FADH2-dependent hydroxylation of putrescine to give N-hydroxyputrescine. PubB can catalyze succinyl-CoA dependent succinylation of N-hydroxyputrescine to give N-hydroxy-N-succinyl-putrescine (HSP), and PubC can catalyze ATP-dependent head-to-tail dimerization of HSP to give pre-putrebactin and subsequent macrocyclization of pre-putrebactin to give putrescine
metabolism
Shewanella algae B516
-
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
Shewanella algae MR-4
-
pubABC encode the enzymes required to assemble putrebactin from putrescine. PubA catalyzes the O2- and FADH2-dependent hydroxylation of putrescine to give N-hydroxyputrescine. PubB can catalyze succinyl-CoA dependent succinylation of N-hydroxyputrescine to give N-hydroxy-N-succinyl-putrescine (HSP), and PubC can catalyze ATP-dependent head-to-tail dimerization of HSP to give pre-putrebactin and subsequent macrocyclization of pre-putrebactin to give putrescine
-
metabolism
Shewanella algae MR-7
-
pubABC encode the enzymes required to assemble putrebactin from putrescine. PubA catalyzes the O2- and FADH2-dependent hydroxylation of putrescine to give N-hydroxyputrescine. PubB can catalyze succinyl-CoA dependent succinylation of N-hydroxyputrescine to give N-hydroxy-N-succinyl-putrescine (HSP), and PubC can catalyze ATP-dependent head-to-tail dimerization of HSP to give pre-putrebactin and subsequent macrocyclization of pre-putrebactin to give putrescine
-
metabolism
-
pubABC encode the enzymes required to assemble putrebactin from putrescine. PubA catalyzes the O2- and FADH2-dependent hydroxylation of putrescine to give N-hydroxyputrescine. PubB can catalyze succinyl-CoA dependent succinylation of N-hydroxyputrescine to give N-hydroxy-N-succinyl-putrescine (HSP), and PubC can catalyze ATP-dependent head-to-tail dimerization of HSP to give pre-putrebactin and subsequent macrocyclization of pre-putrebactin to give putrescine
-
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
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
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pubC, 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 TOP10
gene bibC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli TOP10
gene pubC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli TOP10
gene pubC, recombinant His6-tagged enzyme overexpression in Escherichia coli strain BL21star(DE3)
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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.; Arbache, S.; Song, L.; Oves-Costales, D.; Challis, G.
Identification of a gene cluster that directs putrebactin biosynthesis in Shewanella species PubC catalyzes cyclodimerization of N-hydroxy-N-succinylputrescine
J. Am. Chem. Soc.
130
10458-10459
2008
Shewanella algae (A0AAD1K9Y4), Shewanella putrefaciens (E6XQK0), Shewanella sp., Shewanella algae MR-4 (A0AAD1K9Y4), Shewanella algae MR-7 (A0AAD1K9Y4), Shewanella putrefaciens 200 (E6XQK0)
brenda
EXTERNAL LINKS (specific for EC-Number 6.3.2.63)
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