PMID- 11134965
OWN - NLM
STAT- MEDLINE
DCOM- 20010510
LR  - 20190513
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 129
IP  - 1
DP  - 2001 Jan
TI  - The mtaA gene of the myxothiazol biosynthetic gene cluster from Stigmatella 
      aurantiaca DW4/3-1 encodes a phosphopantetheinyl transferase that activates 
      polyketide synthases and polypeptide synthetases.
PG  - 119-24
AB  - Myxothiazol is synthesized by the myxobacterium Stigmatella aurantiaca DW4/3-1 
      via a combined polyketide synthase/polypeptide synthetase. The biosynthesis of 
      this secondary metabolite is also dependent on the gene product of mtaA. The 
      deduced amino acid sequence of mtaA shows similarity to 4'-phosphopantetheinyl 
      transferases (4'-PP transferase). This points to an enzyme activity that converts 
      inactive forms of the acyl carrier protein domains of polyketide synthetases 
      (PKSs) and/or the peptidyl carrier protein domains of nonribosomal polypeptide 
      synthetases (NRPSs) of the myxothiazol synthetase complex to their corresponding 
      holo-forms. Heterologous co-expression of MtaA with an acyl carrier protein 
      domain of the myxothiazol synthetase was performed in Escherichia coli. The 
      proposed function as a 4'-PP transferase was confirmed and emphasizes the 
      significance of MtaA for the formation of a catalytically active myxothiazol 
      synthetase complex. Additionally, it is shown that MtaA has a relaxed substrate 
      specificity: it processes an aryl carrier protein domain derived from the 
      enterobactin synthetase of E. coli (ArCP) as well as a peptidyl carrier protein 
      domain from a polypeptide synthetase of yet unknown function from Sorangium 
      cellulosum. Therefore, MtaA should be a useful tool for activating heterologously 
      expressed PKS and NRPS systems.
FAU - Gaitatzis, N
AU  - Gaitatzis N
AD  - German Research Centre for Biotechnology, Mascheroder Weg D-38124 Braunschweig, 
      Germany.
FAU - Hans, A
AU  - Hans A
FAU - Muller, R
AU  - Muller R
FAU - Beyer, S
AU  - Beyer S
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Bacterial Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Methacrylates)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Thiazoles)
RN  - 0 (phosphopantetheinyl transferase)
RN  - 6VY98BQ7NB (myxothiazol)
RN  - EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups))
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 6.3.2.- (Peptide Synthases)
SB  - IM
MH  - Adenosine Triphosphatases/*genetics/metabolism
MH  - Amino Acid Sequence
MH  - *Bacterial Proteins
MH  - Carrier Proteins/*genetics/metabolism
MH  - Cloning, Molecular
MH  - Enzyme Activation
MH  - Gene Expression Regulation, Bacterial
MH  - Methacrylates
MH  - Molecular Sequence Data
MH  - Multienzyme Complexes/*metabolism
MH  - Multigene Family
MH  - Peptide Synthases/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Stigmatella aurantiaca/enzymology/*genetics
MH  - Substrate Specificity
MH  - Thiazoles/*metabolism
MH  - *Transferases (Other Substituted Phosphate Groups)
EDAT- 2001/01/03 11:00
MHDA- 2001/05/22 10:01
CRDT- 2001/01/03 11:00
PHST- 2001/01/03 11:00 [pubmed]
PHST- 2001/05/22 10:01 [medline]
PHST- 2001/01/03 11:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a002821 [doi]
PST - ppublish
SO  - J Biochem. 2001 Jan;129(1):119-24. doi: 10.1093/oxfordjournals.jbchem.a002821.