LIVIVO - Search results -

Search results

Result 1 - 10 of total 17

Search options

Article ; Online: Functional chararacterization of the enzymes TabB and TabD involved in tabtoxin biosynthesis by Pseudomonas syringae.

Manning, Margot E / Danson, Eli J / Calderone, Christopher T

Biochemical and biophysical research communications

2018 Volume 496, Issue 1, Page(s) 212–217

Abstract: Pseudomonas syringae pv. tabaci ATCC 11528 produces tabtoxin, a β-lactam-containing dipeptide phytotoxin. Tabtoxinine-β-lactam (TβL), one of tabtoxin's constituent amino acids, structurally mimics lysine, and many of the proteins encoded by the tabtoxin ... ...

Abstract	Pseudomonas syringae pv. tabaci ATCC 11528 produces tabtoxin, a β-lactam-containing dipeptide phytotoxin. Tabtoxinine-β-lactam (TβL), one of tabtoxin's constituent amino acids, structurally mimics lysine, and many of the proteins encoded by the tabtoxin biosynthetic gene cluster are homologs of lysine biosynthetic enzymes, suggesting that the tabtoxin and lysine biosynthetic routes parallel one another. We cloned and expressed TabB and TabD, predicted homologs of tetrahydrodipicolinate (THDPA)-N-acyltransferase and N-acyl-THDPA aminotransferase, respectively, to determine their activities in vitro. We confirmed that TabB succinylates THDPA and that TabD is a PLP-dependent aminotransferase that utilizes glutamate as an amine donor. Surprisingly, we also found that though TabD could utilize the TabB product N-succinyl-THDPA as a substrate, THDPA itself was also recognized. These observations reveal that TabB functionally duplicates DapD, the THDPA-N-succinyltransferase involved in lysine biosynthesis, and reinforce the close relationship between the metabolic logics underpinning the respective biosynthetic pathways.
MeSH term(s)	Acetyltransferases/chemistry ; Acetyltransferases/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Dipeptides/biosynthesis ; Enzyme Activation ; Enzyme Stability ; Pseudomonas syringae/metabolism ; Structure-Activity Relationship ; Transaminases/chemistry ; Transaminases/metabolism
Chemical Substances	Bacterial Proteins ; Dipeptides ; Acetyltransferases (EC 2.3.1.-) ; TabB protein, Pseudomonas syringae (EC 2.3.1.-) ; Transaminases (EC 2.6.1.-) ; tabtoxin (H3YX70R64N)
Language	English
Publishing date	2018--29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2018.01.028
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 116: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾

Article: Isoprenoid-like alkylations in polyketide biosynthesis.

Calderone, Christopher T

Natural product reports

2008 Volume 25, Issue 5, Page(s) 845–853

Abstract: Polyketides are secondary metabolites biosynthesized by the iterative Claisen condensation of malonate units. Despite utilizing only a small set of biochemical transformations, the polyketide biosynthetic machinery yields products of striking structural ... ...

Abstract	Polyketides are secondary metabolites biosynthesized by the iterative Claisen condensation of malonate units. Despite utilizing only a small set of biochemical transformations, the polyketide biosynthetic machinery yields products of striking structural complexity and diversity. Recently, a new polyketide alkylation pathway was characterized that allows access to "beta-branched" structures. This Highlight will describe this alkylation sequence, with special emphasis on its parallels to isoprenoid biosynthesis from primary metabolism and the scope of structures accessible via this pathway.
MeSH term(s)	Alkylation ; Molecular Structure ; Polyketide Synthases/metabolism ; Terpenes/chemistry ; Terpenes/metabolism
Chemical Substances	Terpenes ; Polyketide Synthases (79956-01-7)
Language	English
Publishing date	2008-10
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b807243d
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: ORF7 from Amycolatopsis orientalis catalyzes decarboxylation of N

Kingston, Natalie L / Liu, Yun / Calderone, Christopher T

Biochimica et biophysica acta. Proteins and proteomics

2016 Volume 1865, Issue 1, Page(s) 99–106

Abstract: A key step in the biosynthesis of the polyene polyketide ECO-0501 by Amycolatopsis orientalis ATCC 43491 is thought to involve oxidative decarboxylation of arginine or ... ...

Abstract	A key step in the biosynthesis of the polyene polyketide ECO-0501 by Amycolatopsis orientalis ATCC 43491 is thought to involve oxidative decarboxylation of arginine or N
MeSH term(s)	Actinobacteria/enzymology ; Amides/metabolism ; Arginine/metabolism ; Bacterial Proteins/metabolism ; Biocatalysis ; Carboxy-Lyases/metabolism ; Decarboxylation ; Fatty Acids, Unsaturated/biosynthesis ; Guanidines ; Models, Molecular ; Oxidation-Reduction ; omega-N-Methylarginine/metabolism
Chemical Substances	13-hydroxy-2,12,14,16,22-pentamethyl-28-(N-methyl-guanidino)-octacosa-2,4,6,8,10,14,20,24-octaenoic acid (2-hydroxy-5-oxo-cyclopent-1-enyl)-amide ; Amides ; Bacterial Proteins ; Fatty Acids, Unsaturated ; Guanidines ; omega-N-Methylarginine (27JT06E6GR) ; Arginine (94ZLA3W45F) ; Carboxy-Lyases (EC 4.1.1.-)
Language	English
Publishing date	2016-09-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2016.09.018
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Isoprenoid-like alkylations in polyketide biosynthesis

Calderone, Christopher T.

Natural product reports. 2008 Sept. 26, v. 25, no. 5

2008

Abstract	Polyketides are secondary metabolites biosynthesized by the iterative Claisen condensation of malonate units. Despite utilizing only a small set of biochemical transformations, the polyketide biosynthetic machinery yields products of striking structural complexity and diversity. Recently, a new polyketide alkylation pathway was characterized that allows access to “β-branched” structures. This Highlight will describe this alkylation sequence, with special emphasis on its parallels to isoprenoid biosynthesis from primary metabolism and the scope of structures accessible via this pathway.
Keywords	alkylation ; biosynthesis ; condensation reactions ; isoprenoids ; polyketides ; secondary metabolites
Language	English
Dates of publication	2008-0926
Size	p. 845-853.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b807243d
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article: Small-molecule diversification from iterated branching reaction pathways enabled by DNA-templated synthesis.

Calderone, Christopher T / Liu, David R

Angewandte Chemie (International ed. in English)

2005 Volume 44, Issue 45, Page(s) 7383–7386

MeSH term(s)	Amines/chemical synthesis ; Amines/chemistry ; DNA Primers/chemistry ; Molecular Structure ; Molecular Weight
Chemical Substances	Amines ; DNA Primers
Language	English
Publishing date	2005-12-01
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.200502899
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article: Nucleic-acid-templated synthesis as a model system for ancient translation.

Calderone, Christopher T / Liu, David R

Current opinion in chemical biology

2004 Volume 8, Issue 6, Page(s) 645–653

Abstract: The translation of nucleic acids into synthetic structures with expanded functional potential has been the subject of considerable research, with applications including small-molecule and polymer evolution, reaction discovery and sensing. Here, we review ...

Abstract	The translation of nucleic acids into synthetic structures with expanded functional potential has been the subject of considerable research, with applications including small-molecule and polymer evolution, reaction discovery and sensing. Here, we review properties of nucleic-acid-templated synthesis in the context of requirements for prebiotic translation. This analysis highlights the chemical possibilities of ancient translation systems, as well as challenges that these systems may have faced.
MeSH term(s)	DNA/chemistry ; Evolution, Molecular ; Models, Chemical ; Nucleic Acids/chemical synthesis ; Nucleic Acids/chemistry ; Protein Biosynthesis ; Templates, Genetic
Chemical Substances	Nucleic Acids ; DNA (9007-49-2)
Language	English
Publishing date	2004-12
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1439176-4
ISSN	1879-0402 ; 1367-5931
ISSN (online)	1879-0402
ISSN	1367-5931
DOI	10.1016/j.cbpa.2004.09.003
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 4986: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: FenF: servicing the Mycosubtilin synthetase assembly line in trans.

Aron, Zachary D / Fortin, Pascal D / Calderone, Christopher T / Walsh, Christopher T

Chembiochem : a European journal of chemical biology

2007 Volume 8, Issue 6, Page(s) 613–616

MeSH term(s)	Antifungal Agents/biosynthesis ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/biosynthesis ; Bacterial Proteins/genetics ; Carrier Proteins/chemistry ; Cloning, Molecular ; DNA, Bacterial/genetics ; Escherichia coli/metabolism ; Genes, Bacterial/genetics ; Lipoproteins/biosynthesis ; Lipoproteins/genetics ; Multienzyme Complexes/genetics ; Plasmids ; Recombinant Proteins/chemistry
Chemical Substances	Antifungal Agents ; Bacterial Proteins ; Carrier Proteins ; DNA, Bacterial ; Lipoproteins ; Multienzyme Complexes ; Recombinant Proteins ; mycosubtilin synthetase ; mycosubtiline (1392-60-5)
Language	English
Publishing date	2007-04-16
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.200600575
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis.

Bumpus, Stefanie B / Magarvey, Nathan A / Kelleher, Neil L / Walsh, Christopher T / Calderone, Christopher T

Journal of the American Chemical Society

2008 Volume 130, Issue 35, Page(s) 11614–11616

Abstract: Polyketide biosynthesis is typically directed by cis-acting catalytic domains. In the case of the Bacillus subtilis secondary metabolite dihydrobacillaene, the cis-acting domains are not sufficient to generate the saturated C14'-C15' bond. In this ... ...

Abstract	Polyketide biosynthesis is typically directed by cis-acting catalytic domains. In the case of the Bacillus subtilis secondary metabolite dihydrobacillaene, the cis-acting domains are not sufficient to generate the saturated C14'-C15' bond. In this communication, we identify PksE as a trans-acting enoyl reductase utilized in the biosynthesis of this portion of dihydrobacillaene. PksE is homologous to the enzymes predicted to serve as enoyl reductases in polyunsaturated fatty acid (PUFA) biosynthesis, and we confirmed this functional assignment in vitro. These results suggest a general enoyl reduction pathway in polyketide biosynthesis and a means by which PUFA-like biosynthetic machinery can modulate small-molecule function.
MeSH term(s)	Bacillus subtilis/enzymology ; Fatty Acids, Unsaturated/chemistry ; Fatty Acids, Unsaturated/metabolism ; Macrolides/chemistry ; Macrolides/metabolism ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Polyketide Synthases/chemistry ; Polyketide Synthases/metabolism
Chemical Substances	Fatty Acids, Unsaturated ; Macrolides ; Polyketide Synthases (79956-01-7) ; Oxidoreductases (EC 1.-)
Language	English
Publishing date	2008-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/ja8040042
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A ketoreductase domain in the PksJ protein of the bacillaene assembly line carries out both alpha- and beta-ketone reduction during chain growth.

Calderone, Christopher T / Bumpus, Stefanie B / Kelleher, Neil L / Walsh, Christopher T / Magarvey, Nathan A

Proceedings of the National Academy of Sciences of the United States of America

2008 Volume 105, Issue 35, Page(s) 12809–12814

Abstract: The polyketide signaling metabolites bacillaene and dihydrobacillaene are biosynthesized in Bacillus subtilis on an enzymatic assembly line with both nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) modules acting along with catalytic ...

Abstract	The polyketide signaling metabolites bacillaene and dihydrobacillaene are biosynthesized in Bacillus subtilis on an enzymatic assembly line with both nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) modules acting along with catalytic domains servicing the assembly line in trans. These signaling metabolites possess the unusual starter unit alpha-hydroxyisocaproate (alpha-HIC). We show here that it arises from initial activation of alpha-ketoisocaproate (alpha-KIC) by the first adenylation domain of PksJ (a hybrid PKS/NRPS) and installation on the pantetheinyl arm of the adjacent thiolation (T) domain. The alpha-KIC unit is elongated to alpha-KIC-Gly by the second NRPS module in PksJ as demonstrated by mass spectrometric analysis. The third module of PksJ uses PKS logic and contains an embedded ketoreductase (KR) domain along with two adjacent T domains. We show that this KR domain reduces canonical 3-ketobutyryl chains but also the alpha-keto group of alpha-KIC-containing intermediates on the PksJ T-domain doublet. This KR activity accounts for the alpha-HIC moiety found in the dihydrobacillaene/bacillaene pair and represents an example of an assembly-line dual-function alpha- and beta-KR acting on disparate positions of a growing chain intermediate.
MeSH term(s)	Bacillus subtilis/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Chromatography, High Pressure Liquid ; Esters/metabolism ; Keto Acids/metabolism ; Ketones/metabolism ; Oxidation-Reduction ; Polyenes/chemistry ; Polyenes/metabolism ; Protein Structure, Tertiary ; Structure-Activity Relationship
Chemical Substances	Bacterial Proteins ; Esters ; Keto Acids ; Ketones ; Polyenes ; bacillaene ; alpha-ketoisocaproic acid (816-66-0)
Language	English
Publishing date	2008-08-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0806305105
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: A ketoreductase domain in the PksJ protein of the bacillaene assembly line carries out both α- and β-ketone reduction during chain growth

Calderone, Christopher T / Bumpus, Stefanie B / Kelleher, Neil L / Walsh, Christopher T / Magarvey, Nathan A

Proceedings of the National Academy of Sciences of the United States of America. 2008 Sept. 2, v. 105, no. 35

2008

Abstract	The polyketide signaling metabolites bacillaene and dihydrobacillaene are biosynthesized in Bacillus subtilis on an enzymatic assembly line with both nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) modules acting along with catalytic domains servicing the assembly line in trans. These signaling metabolites possess the unusual starter unit α-hydroxyisocaproate (α-HIC). We show here that it arises from initial activation of α-ketoisocaproate (α-KIC) by the first adenylation domain of PksJ (a hybrid PKS/NRPS) and installation on the pantetheinyl arm of the adjacent thiolation (T) domain. The α-KIC unit is elongated to α-KIC-Gly by the second NRPS module in PksJ as demonstrated by mass spectrometric analysis. The third module of PksJ uses PKS logic and contains an embedded ketoreductase (KR) domain along with two adjacent T domains. We show that this KR domain reduces canonical 3-ketobutyryl chains but also the α-keto group of α-KIC-containing intermediates on the PksJ T-domain doublet. This KR activity accounts for the α-HIC moiety found in the dihydrobacillaene/bacillaene pair and represents an example of an assembly-line dual-function α- and β-KR acting on disparate positions of a growing chain intermediate.
Language	English
Dates of publication	2008-0902
Size	p. 12809-12814.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 63/44: Show issues
87/25270: Show issues
Qa 4' 169/3: Show issues
Z 8.7: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

To top

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED