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

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
2.3.1.15 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

EC Number Metals/Ions Comment Organism Structure
2.3.1.15 Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.15 Mycobacterium tuberculosis P9WI59
-
-
2.3.1.15 Mycobacterium tuberculosis ATCC 25618 P9WI59
-
-
2.3.1.15 Mycobacterium tuberculosis H37Rv P9WI59
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.15 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.15 7.5
-
 assay at Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.15 metabolism the enzyme catalyzes the initial step of glycerophospholipid biosynthesis in the mycobacterial cell, pathway overview Mycobacterium tuberculosis
2.3.1.15 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