Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
twitter

MetaCyc Enzyme: acyl-CoA synthetase

Gene: fadD32 Accession Number: RV3801C (MetaCyc)

Species: Mycobacterium tuberculosis H37Rv

Summary:
(MTV026.06c), len: 637. fadD32, similar to gp|Z97188|MTCY409_4 M. tuberculosiscosmid (584 aa). FASTA scores: opt: 1094 z-score: 1262.3 E(): 0, 36.8% identity in 585 aa overlap. Also similar to manyother mycobacterial hypothetical proteins: MTCY9F9_39,MTCY338_18, MTCY349_40, MTV005_21, MBU75685_1 Mycobacterium bovis acyl-CoA ligase, MTCY24G1_8,MTCY19G5_7, MTCY4D9_17

Map Position: [4,261,150 <- 4,263,063] (96.59 centisomes)

Molecular Weight of Polypeptide: 69.232 kD (from nucleotide sequence)

Unification Links: Entrez-gene:886130 , Pride:O53580 , Protein Model Portal:O53580 , SMR:O53580 , String:83332.Rv3801c , UniProt:O53580

Relationship Links: InterPro:IN-FAMILY:IPR000873 , Pfam:IN-FAMILY:PF00501 , Prosite:IN-FAMILY:PS00455

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

MultiFun Terms: metabolism


Enzymatic reaction of: trans-keto-C61-meroacyl-AMP ligase (acyl-CoA synthetase)

EC Number: 6.2.1.-

a trans-keto-C61-meroacyl-[acp] + ATP + H2O <=> a trans-keto-meroacyl-adenylate + a holo-[acyl-carrier protein] + 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 physiologically favored in the direction shown.

In Pathways: superpathway of mycolate biosynthesis , mycolate biosynthesis

Summary:
acyl-CoA synthetase is a very specific fatty acyl-AMP ligase that catalyzes the conversion of each meroacyl-ACP derived from the FAS-II system to meroacyl-AMP [Takayama05]. Enzymatic activity of purified acyl-CoA synthetase of M. tuberculosis catalyzing these reactions were shown by Radio-TLC coupled with HPLC and ESI-MS [Trivedi04].


Enzymatic reaction of: cis-keto-C60-meroacyl-AMP ligase (acyl-CoA synthetase)

EC Number: 6.2.1.-

a cis-keto-C60-meroacyl-[acp] + ATP + H2O <=> a cis-keto-meroacyl-adenylate + a holo-[acyl-carrier protein] + 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 physiologically favored in the direction shown.

In Pathways: superpathway of mycolate biosynthesis , mycolate biosynthesis

Summary:
acyl-CoA synthetase is a very specific fatty acyl-AMP ligase that catalyzes the conversion of each meroacyl-ACP derived from the FAS-II system to meroacyl-AMP [Takayama05]. Enzymatic activity of purified acyl-CoA synthetase of M. tuberculosis catalyzing these reactions were shown by Radio-TLC coupled with HPLC and ESI-MS [Trivedi04].


Enzymatic reaction of: trans-methoxy-C60-meroacyl-AMP ligase (acyl-CoA synthetase)

EC Number: 6.2.1.-

a trans-methoxy-C60-meroacyl-[acp] + ATP + H2O <=> a trans-methoxy-meroacyl-adenylate + a holo-[acyl-carrier protein] + 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 physiologically favored in the direction shown.

In Pathways: superpathway of mycolate biosynthesis , mycolate biosynthesis

Summary:
acyl-CoA synthetase is a very specific fatty acyl-AMP ligase that catalyzes the conversion of each meroacyl-ACP derived from the FAS-II system to meroacyl-AMP [Takayama05]. Enzymatic activity of purified acyl-CoA synthetase of M. tuberculosis catalyzing these reactions were shown by Radio-TLC coupled with HPLC and ESI-MS [Trivedi04].


Enzymatic reaction of: cis-methoxy-C59-meroacyl-AMP ligase (acyl-CoA synthetase)

EC Number: 6.2.1.-

a cis-methoxy-C59-meroacyl-[acp] + ATP + H2O <=> a cis-methoxy-meroacyl-adenylate + a holo-[acyl-carrier protein] + 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 physiologically favored in the direction shown.

In Pathways: superpathway of mycolate biosynthesis , mycolate biosynthesis

Summary:
acyl-CoA synthetase is a very specific fatty acyl-AMP ligase that catalyzes the conversion of each meroacyl-ACP derived from the FAS-II system to meroacyl-AMP [Takayama05]. Enzymatic activity of purified acyl-CoA synthetase of M. tuberculosis catalyzing these reactions were shown by Radio-TLC coupled with HPLC and ESI-MS [Trivedi04].


Enzymatic reaction of: C52-α-meroacyl-AMP ligase (acyl-CoA synthetase)

EC Number: 6.2.1.-

a C52-α-meroacyl-[acp] + ATP + H2O <=> a C52-α-meroacyl-adenylate + a holo-[acyl-carrier protein] + 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 physiologically favored in the direction shown.

In Pathways: superpathway of mycolate biosynthesis , mycolate biosynthesis

Summary:
acyl-CoA synthetase is a very specific fatty acyl-AMP ligase that catalyzes the conversion of each meroacyl-ACP derived from the FAS-II system to meroacyl-AMP [Takayama05]. Enzymatic activity of purified acyl-CoA synthetase of M. tuberculosis catalyzing these reactions were shown by Radio-TLC coupled with HPLC and ESI-MS [Trivedi04].


References

Takayama05: Takayama K, Wang C, Besra GS (2005). "Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis." Clin Microbiol Rev 18(1);81-101. PMID: 15653820

Trivedi04: Trivedi OA, Arora P, Sridharan V, Tickoo R, Mohanty D, Gokhale RS (2004). "Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria." Nature 428(6981);441-5. PMID: 15042094


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 19.0 on Thu Sep 3, 2015, biocyc13.