The involvement of bound-CoA in glyceride biosynthesis

Rao, Govind; Johnston, John M.

doi:10.1016/0006-291x(66)90380-9

Cited by 6 publications

(4 citation statements)

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“…intestine and in the liver of neonatal rats (3,8,9,16,17). Although intense efforts were focused on purification and identification of the gene encoding the enzyme (3,15,18,25), like most biosynthetic enzymes involved in TAG synthesis, it proved difficult to clone the gene encoding MGAT due partly to the nature of the enzyme as a microsome-associated protein (18,26). We have recently reported the cloning and characterization of the first mammalian intestinal MGAT (4), the mouse MGAT2, which has made it possible to clone the homologous genes from other species.…”

Section: E932 Differential Features Of the Human Mgat2mentioning

confidence: 99%

“…Historically, the isolation and characterization of MGAT have been hindered by the fact that the enzyme is an integral membrane protein within intestinal microsomes. There is evidence that MGAT and DGAT along with acyl-CoA ligase may form a "triacylglycerol synthetase complex," thus making the purification and characterization of individual enzymes more difficult (25). Nonetheless, intense efforts have resulted in partial purification and characterization of the MGAT enzyme (3,15,18,25).…”

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confidence: 99%

“…There is evidence that MGAT and DGAT along with acyl-CoA ligase may form a "triacylglycerol synthetase complex," thus making the purification and characterization of individual enzymes more difficult (25). Nonetheless, intense efforts have resulted in partial purification and characterization of the MGAT enzyme (3,15,18,25). We have recently reported the cloning and characterization of the first mammalian intestinal monoacylglycerol acyltransferase, MGAT2, from mouse (4), which has made it possible to clone the gene from other species.…”

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confidence: 99%

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Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity

Lockwood

Cao

Burn

et al. 2003

American Journal of Physiology-Endocrinology and Metabolism

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Acyl CoA-monoacylglycerol acyltransferase (MGAT) catalyzes the first step in triacyglycerol resynthesis involved in dietary absorption in enterocytes. Despite its potentially important role in dietary fat absorption, a gene encoding a human intestinal MGAT has not been identified. In this study, we report the identification and functional characterization of a human intestinal MGAT (hMGAT2) and its splice variant (hMGAT2V). The hMGAT2 gene encodes a peptide of 334 amino acids with a molecular mass of 38.2 kDa that shares 81 and 47% amino acid identities with the mouse MGAT2 and the human diacylglycerol acyltransferase (DGAT2) enzymes, respectively. The hMGAT2 gene is localized on chromosome 11q13.5, adjacent to the DGAT2 gene, suggesting gene duplication. Transient expression of hMGAT2, but not an alternatively spliced variant, hMGAT2V, in COS-7 cells led to a ninefold increase in the synthesis of DAG. The human and mouse differ significantly in tissue distribution of MGAT2. In addition to a predominant expression in the small intestine in both species, distinct levels were also found in the human liver, contrasting with higher levels in the mouse kidney. In comparison with a single 1.8-kb transcript in mouse, the hMGAT2 gene expressed two transcripts of 3.0 and 6.0 kb in size that encode MGAT2 and an inactive peptide with unknown functions, respectively. Despite a significant level of hMGAT2 mRNA in the human liver, little MGAT activity was detected in liver microsomes when tested against monoacyglcerols with different unsaturated side chains, suggesting possible posttranscriptional regulation.

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Section: E932 Differential Features Of the Human Mgat2mentioning

confidence: 99%

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confidence: 99%

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Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity

Lockwood

Cao

Burn

et al. 2003

American Journal of Physiology-Endocrinology and Metabolism

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“…Two forms of the enzyme were assumed to exist, an active one involving enzyme-bound CoA, and an inactive one devoid of CoA. In support of this view Rao & Johnston (1966 reported activation by the simultaneous presence of CoA and ATP of the glyceride synthetase complex isolated from hamster intestine. The enzyme thus activated catalysed the transfer of fatty acid to fatty acid triglyceride in the absence of added CoA, and combination of CoA with the enzyme was suggested.…”

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confidence: 92%

Studies on medium-chain fatty acyl-coenzyme A synthetase. Purification and properties

Bar‐Tana

Rose

Shapiro

1968

Biochemical Journal

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1. Medium-chain fatty acyl-CoA synthetase (EC 6.2.1.2) was isolated by the method of Mahler, Wakil & Bock (1953) and the enzyme activity determined by the disappearance of CoA in the presence either of butyrate and ATP or of butyryl-AMP, as well as by ATP formation from butyryl-AMP and PP(i). 2. Preincubation of the enzyme with CoA and ATP alone or together, followed by the removal of these substrates by gel filtration, caused a marked inhibition of ATP formation, contrary to results previously obtained with palmitoyl-CoA synthetase. 3. The effect of ATP on butyryl-AMP-dependent CoA disappearance was inconsistent. Low concentrations of ATP (0.1-0.5mm) always caused inhibition, whereas higher concentrations (5-10mm) activated in some enzyme preparations and inhibited in others. 4. This inconsistency was shown to be due to the presence of two enzyme fractions. Both fractions had similar activities when assayed by the butyryl-AMP- or butyrate-plus-ATP-dependent CoA disappearance. However, fraction I was activated by ATP as measured by butyryl-AMP-dependent CoA disappearance whereas fraction II was inhibited by it. Fraction I also catalysed ATP formation from butyryl-AMP and PP(i) whereas fraction II was lacking in such activity. 5. The relationship of these observations with respect to other known mechanisms of fatty acid-activating systems is discussed.

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Gastrointestinal Tissue

Johnston

1977

Lipid Metabolism in Mammals

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The involvement of bound-CoA in glyceride biosynthesis

Cited by 6 publications

References 5 publications

Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity

Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity

Studies on medium-chain fatty acyl-coenzyme A synthetase. Purification and properties

Gastrointestinal Tissue

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