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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: phosphate propanoyltransferase

Gene: pduL Accession Number: G-15050 (MetaCyc)

Species: Salmonella enterica enterica serovar Typhimurium str. LT2

Summary:
The subunit structurer of this enzyme has not been reported. The apparent molecular mass of the C-terminal His8-tagged fusion protein was determined by SDS-PAGE [Liu07].

This enzyme catalyzes the production of propanoyl phosphate from propanoyl-CoA in pathway L-1,2-propanediol degradation. It was described as an evolutionarily distinct enzyme that is unrelated in amino acid sequence to known phosphotransacylase enzymes. Homologs of PduL appear to be absent in archaea and eukaryotes.

Mutant studies showed that pduL mutants are impaired for aerobic growth on (S)-propane-1,2-diol and are unable to utilize it under fermentation conditions. PduL also had phosphate acetyltransferase activity and could correct the growth defect of a pta mutant, allowing growth on acetate. However, although Pta has a phosphate propanoyltransferase activity, it could not substitute for PduL [Liu07].

Recombinant enzyme was overexpressed in Escherichia coli as a C-terminal His8-tagged fusion protein, purified and characterized kinetically [Liu07].

Gene Citations: [Bobik99, Bobik97]

Map Position: [2,123,805 -> 2,124,437]

Molecular Weight of Polypeptide: 22.972 kD (from nucleotide sequence), 27.0 kD (experimental) [Liu07 ]

Unification Links: Entrez-gene:1253568 , Pride:Q9XDN5 , String:99287.STM2047 , UniProt:Q9XDN5

Relationship Links: InterPro:IN-FAMILY:IPR008300 , Pfam:IN-FAMILY:PF06130

Gene-Reaction Schematic: ?

Credits:
Created 20-Mar-2012 by Fulcher CA , SRI International


Enzymatic reaction of: phosphate acetyltransferase (phosphate propanoyltransferase)

EC Number: 2.3.1.8

acetyl-CoA + phosphate <=> acetyl phosphate + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible. [Liu07]

Kinetic Parameters:

Substrate
Km (μM)
Citations
acetyl phosphate
970.0
[Liu07]


Enzymatic reaction of: phosphate propanoyltransferase

Synonyms: phosphate acyltransferase, phosphotransacylase

EC Number: 2.3.1.222

propanoyl-CoA + phosphate <=> propanoyl phosphate + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible. [Liu07]

In Pathways: L-1,2-propanediol degradation , threonine degradation I

Summary:
propanoyl-CoA was identified by HPLC and mass spectrometry as a product of the reverse reaction [Liu07].

Kinetic analysis showed that the purified, C-terminal His8-tagged recombinant protein was 3.8-fold more active with propanoyl phosphate than with acetyl phosphate as substrate [Liu07].

Kinetic Parameters:

Substrate
Km (μM)
Citations
propanoyl phosphate
610.0
[Liu07]


References

Bobik97: Bobik TA, Xu Y, Jeter RM, Otto KE, Roth JR (1997). "Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes for the propanediol dehydratase." J Bacteriol 179(21);6633-9. PMID: 9352910

Bobik99: Bobik TA, Havemann GD, Busch RJ, Williams DS, Aldrich HC (1999). "The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation." J Bacteriol 181(19);5967-75. PMID: 10498708

Liu07: Liu Y, Leal NA, Sampson EM, Johnson CL, Havemann GD, Bobik TA (2007). "PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2." J Bacteriol 189(5);1589-96. PMID: 17158662


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.