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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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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: ?

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 18.5 on Sat Dec 20, 2014, BIOCYC14B.