Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: achromobactin synthetase protein D

Gene: Psyr2584 Accession Number: G-12140 (MetaCyc)

Synonyms: acsD

Species: Pseudomonas syringae pv. syringae B728a

Summary:
The subunit structure of this enzyme has not been reported.

This enzyme is a member of the NIS synthetase superfamily, a conserved group of enzymes catalyzing adenylation and condensation reactions. NIS synthetases are structurally distinct from the non-ribosomal peptide synthetases (NRPS). NIS (NRPS-independent) synthetases are involved in siderophore biosynthesis. They activate carboxylic acid substrates by forming acid adenylates in a mechanism distinct from NRPS enzymes. Based on bioinformatic analyses there are three proposed subclasses within the NIS superfamily depending upon the type of carboxylic acid substrate that is activated. Type A NIS synthetases recognize one of the pro-chiral groups of citrate. Type B NIS synthetases recognize the δ-acid group of 2-oxoglutarate (α-ketoglutarate). Type C NIS synthetases recognize esterified or amidated derivatives of carboxylic acids (in [Berti09a]).

Recombinant, hexahistidine-tagged protein was overexpressed in Escherichia coli and purified [Berti09a].

Gene Citations: [Feil05]

Unification Links: Entrez:AAY37623

Relationship Links: Entrez-Nucleotide:PART-OF:CP000075

Gene-Reaction Schematic: ?

Credits:
Created 13-Aug-2010 by Fulcher CA , SRI International


Enzymatic reaction of: citrate:ethanolamine ligase (achromobactin synthetase protein D)

citrate + ATP + ethanolamine <=> O-citryl-ethanolamine + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: achromobactin biosynthesis

Summary:
The enzyme was assayed for activation of citrate, or 2-oxoglutarate using a method that detects hydroxamates formed from the reaction between activated carboxylic acids and hydroxylamine. For AcsD, hydroxamates were formed upon incubation with citrate [Berti09a].

Cofactors or Prosthetic Groups: Mg2+ [Berti09a]

Kinetic Parameters:

Substrate
Km (μM)
Citations
citrate
1900.0
[Berti09a]


References

Berti09a: Berti AD, Thomas MG (2009). "Analysis of achromobactin biosynthesis by Pseudomonas syringae pv. syringae B728a." J Bacteriol 191(14);4594-604. PMID: 19482931

Feil05: Feil H, Feil WS, Chain P, Larimer F, DiBartolo G, Copeland A, Lykidis A, Trong S, Nolan M, Goltsman E, Thiel J, Malfatti S, Loper JE, Lapidus A, Detter JC, Land M, Richardson PM, Kyrpides NC, Ivanova N, Lindow SE (2005). "Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000." Proc Natl Acad Sci U S A 102(31);11064-9. PMID: 16043691


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc14.