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: glucosamine-1-phosphate guanylyltransferase

Gene: ptmE Accession Number: G-12602 (MetaCyc)

Synonyms: Cj1329

Species: Campylobacter jejuni jejuni NCTC 11168 = ATCC 700819

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

In the food-borne pathogen Campylobacter jejuni this enzyme participates in the biosynthesis of CMP-N,N'-diacetyllegionaminate (CMP-legionaminic acid), a virulence-associated, cell surface sialic acid-like derivative (see pathway CMP-legionaminate biosynthesis I). PtmE is a nucleotidyltransferase with an absolute specificity for GTP when D-glucosamine 1-phosphate is the substrate. This allowed large-scale purification of GDP-D-glucosamine) [Schoenhofen09].

Recombinant, N-terminal His6-tagged polypeptide was purified and characterized. The ptmE gene sequence contained a CBS domain of unknown function [Schoenhofen09].

In "one pot" enzymatic reactions, PtmF, PtmA, PgmL and PtmE converted β-D-fructofuranose 6-phosphate to GDP-D-glucosamine in the CMP-legionaminic acid biosynthetic pathway. Metabolites were purified and identified by capillary electrophoresis/mass spectrometry analysis and NMR spectroscopy [Schoenhofen09].

Map Position: [1,256,292 -> 1,257,317]

Molecular Weight of Polypeptide: 38.839 kD (from nucleotide sequence)

Unification Links: Entrez-gene:905621 , Protein Model Portal:Q0P8S9 , String:192222.Cj1329 , UniProt:Q0P8S9

Relationship Links: InterPro:IN-FAMILY:IPR000644 , InterPro:IN-FAMILY:IPR005835 , Pfam:IN-FAMILY:PF00483 , Pfam:IN-FAMILY:PF00571 , Prosite:IN-FAMILY:PS51371 , Smart:IN-FAMILY:SM00116

Gene-Reaction Schematic: ?

Credits:
Created 15-Mar-2011 by Fulcher CA , SRI International


Enzymatic reaction of: glucosamine-1-phosphate guanylyltransferase

EC Number: 2.7.7.-

D-glucosamine 1-phosphate + GTP + H+ <=> GDP-D-glucosamine + 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.

Alternative Substrates for D-glucosamine 1-phosphate: α-D-glucose 1-phosphate [Schoenhofen09 ] , N-acetyl-α-D-glucosamine 1-phosphate [Schoenhofen09 ]

In Pathways: CMP-legionaminate biosynthesis I

Summary:
This nucleotidyltransferase showed an absolute specificity for GTP as donor when D-glucosamine 1-phosphate was used as acceptor. The enzyme was specific for the C4 configuration of D-glucose. galactosamine-1-phosphate was not a substrate. When N-acetyl-α-D-glucosamine 1-phosphate was used as acceptor, the enzyme showed more promiscuity with regard to NTP donors [Schoenhofen09].


References

Schoenhofen09: Schoenhofen IC, Vinogradov E, Whitfield DM, Brisson JR, Logan SM (2009). "The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors." Glycobiology 19(7);715-25. PMID: 19282391


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 Thu Dec 18, 2014, BIOCYC13B.