Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.48 extracted from

  • Rittershaus, E.S.C.; Baek, S.H.; Krieger, I.V.; Nelson, S.J.; Cheng, Y.S.; Nambi, S.; Baker, R.E.; Leszyk, J.D.; Shaffer, S.A.; Sacchettini, J.C.; Sassetti, C.M.
    A lysine acetyltransferase contributes to the metabolic adaptation to hypoxia in Mycobacterium tuberculosis (2018), Cell Chem. Biol., 25, 1495-1505.e3 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.48

Activating Compound

Activating Compound Comment Organism Structure
cAMP Pat is a cAMP-regulated protein lysine acetyltransferase, that contains an additional nucleotide-binding domain that is structurally similar to the cAMP responsive region of protein kinase A, and inhibits acetyltransferase activity until cAMP is bound Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis O05581
-
-
Mycobacterium tuberculosis ATCC 25618 O05581
-
-
Mycobacterium tuberculosis H37Rv O05581
-
-

Synonyms

Synonyms Comment Organism
cAMP-regulated protein lysine acetyltransferase
-
 Mycobacterium tuberculosis
GCN5-like enzyme UniProt Mycobacterium tuberculosis
GCN5-related N-acetyltransferase UniProt Mycobacterium tuberculosis
GNAT UniProt Mycobacterium tuberculosis
MtPat
-
 Mycobacterium tuberculosis
Pat
-
 Mycobacterium tuberculosis
protein acetyl-transferase
-
 Mycobacterium tuberculosis
Rv0998
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
malfunction profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability Mycobacterium tuberculosis
physiological function protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions Mycobacterium tuberculosis