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

BRENDA support

Literature summary for 2.3.1.15 extracted from

  • Law, J.D.; Daniel, J.
    The mycobacterial Rv1551 glycerol-3-phosphate acyltransferase enhances phospholipid biosynthesis in cell lysates of Escherichia coli (2017), Microb. Pathog., 113, 269-275 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene plsB1 or Rv1551, DNA and amino acid sequence determination and analysis, sequence comparisons, subcloning in Escherichia coli strain TOP10, functional recombinant expression in Escherichia coli strain BL21 Star (DE3) leading to significantly (2-4fold) higher viable cell counts during the exponential and stationary phases. Growth of Escherichia coli in medium containing long-chain fatty acids is enhanced by mGPAT. The enzyme displays function as a GPAT by enhancing the synthesis of phospholipids from exogenously provided fatty acids in Escherichia coli cell lysates Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate Mycobacterium tuberculosis
-
CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate Mycobacterium tuberculosis H37Rv
-
CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate Mycobacterium tuberculosis ATCC 25618
-
CoA + 1-acyl-sn-glycerol 3-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WI59
-
-
Mycobacterium tuberculosis ATCC 25618 P9WI59
-
-
Mycobacterium tuberculosis H37Rv P9WI59
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate
-
Mycobacterium tuberculosis CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate
-
Mycobacterium tuberculosis H37Rv CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate
-
Mycobacterium tuberculosis ATCC 25618 CoA + 1-acyl-sn-glycerol 3-phosphate
-
?

Subunits

Subunits Comment Organism
? x * 69000, recombinant detagged enzyme, SDS-PAGE, x * 72000, recombinant tagged enzyme, SDS-PAGE Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
glycerol-3-phosphate acyltransferase
-
Mycobacterium tuberculosis
GPAT
-
Mycobacterium tuberculosis
mGPAT
-
Mycobacterium tuberculosis
PlsB1
-
Mycobacterium tuberculosis
Rv1551
-
Mycobacterium tuberculosis
Rv1551 acyltransferase
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the initial step of glycerophospholipid biosynthesis in the mycobacterial cell, pathway overview Mycobacterium tuberculosis
physiological function glycerol-3-phosphate acyltransferase (GPAT) catalyzes the first step of the glycerophospholipid biosynthetic pathway that synthesizes the lipid precursors for triacylglycerol biosynthesis. GPAT catalyzes the acylation of glycerol-3-phosphate to form lysophosphatidic acid. Role of GPAT in dormancy-associated triacylglycerol synthesis in Mycobacterium tuberculosis Mycobacterium tuberculosis