Biosynthesis of porphyrin precursors: Kinetic studies on mammalian l-alanine: γ,δ-Dioxovaleric acid aminotransferase

Varticovski, Lyuba; Kushner, James P.; Burnham, Bruce F.

doi:10.1016/0020-711x(80)90155-x

Cited by 14 publications

(11 citation statements)

References 13 publications

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“…These data indicate that under the conditions of these experiments, DOVA and glycine are converted to hepatic heme with similar efficiency. Previous in vitro studies suggested that the efficiency of conversion of DOVA to tetrapyrroles was greater than that of glycine (8). Failure to observe more efficient hepatic utilization of DOVA in the whole-animal experiments is unexplained but may reflect a combination of partial inhibition by DOVA of the cytosolic enzyme ALA dehydrase and differences in permeability between the cell and mitochondrial membranes.…”

Section: Resultsmentioning

confidence: 91%

“…1B). The capacity of the L-alanine: DOVA aminotransferase reaction to synthesize ALA appeared to exceed that of the ALA synthase reaction (8). Finally, we have presented in vitro evidence for the conversion of DOVA to porphyrins and heme in suspensions of intact, respiring rat hepatocytes (10).…”

Section: Introductionmentioning

confidence: 86%

“…Similar transamination reactions have also been demonstrated in algae and bacteria (6,7). We recently reported the isolation and characterization of an enzyme from bovine liver mitochondria that synthesizes ALA by a transamination reaction (8,9). This enzyme, L-alanine: 4,5-dioxovaleric acid aminotransferase, catalyzes a transamination reaction between L-alanine and 4,5-dioxovalerate (DOVA), yielding ALA and pyruvate (Fig.…”

Section: Introductionmentioning

confidence: 99%

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Biosynthesis of 5-aminolevulinic acid and heme from 4,5-dioxovalerate in the rat.

Morton¹,

Kushner²,

Straka³

et al. 1983

J. Clin. Invest.

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A B S T R A C T We previously demonstrated an alternate pathway for the biosynthesis of 5-aminolevulinic acid (ALA) in bovine liver mitochondria and of tetrapyrroles in suspensions of rat hepatocytes (1980. J. Biol. Chem. 255: 3742;. Proc. Natl. Acad. Sci. USA. 78: 5335). This pathway involves a transamination reaction that incorporates the intact 5-carbon skeleton of 4,5-dioxovaleric acid (DOVA) into ALA.We investigated this alternate pathway in vivo by the intraperitoneal injection of DOVA into rats. 3.4%, respectively, of the radioactivity as hepatic heme after 3 h. These doses of radiolabeled DOVA, glycine, and ALA were injected into rats with phenylhydrazine-induced anemia. Recovery of radioactivity after 3 h as splenic (erythroid) heme was 0.35% for DOVA, 0.072% for glycine, and 0.25% for ALA. These studies establish that the intact 5-carbon skeleton of DOVA can be incorporated into ALA and heme in vivo.

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Section: Resultsmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biosynthesis of 5-aminolevulinic acid and heme from 4,5-dioxovalerate in the rat.

Morton¹,

Kushner²,

Straka³

et al. 1983

J. Clin. Invest.

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“…Two possible pathways for 6 -a m i n o l e~c acid (= 5-aminolevulinic acid, ALA) formatlon idenbfled in the mitochondria of animal tissue (upper) and plant tissue (lower). Varticovski et al (1980) have found indications of the 'glutamate' pathway in bovine hepatic tissue as well. According to present knowledge, the further condensation of 2 molecules of ALA to porphobilinogen (PBG) is catalyzed by the enzyme ALA-D (= PBG synthase), and protoporphyrin is formed after 5 further specific reactions.…”

Section: Resultsmentioning

confidence: 99%

Effects of mercury on physiological condition and content of the biomarker ALA in the oyster Ostrea edulis

Brock¹

1993

Mar. Ecol. Prog. Ser.

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Ostrea edulis (L.) exposed to mercury in situ at Chemlnova In the western part of Nissum Bredning, Limfjord, Denmark, was compared to a non-exposed oyster sample from the uncontaminated eastern part of the area A similar comparison was made for oysters, exposed and non-exposed to Hg, in the laboratory. Comparisons were based on stepwise multiple regression analysis, and MANOVA, using these variables. shell length, volume between shell valves, tissue dry weight, length and width of shell muscle scar, and infection by the parasite B0nam.a ostreae (determined by ELISA). For the environmental as well as for the laboratory samples, no significant differences between exposed and non-exposed oysters were found. The content of the biomarker 6-aminolevulin~c acid (ALA) was detected by ion-exchange chromatography in all samples. ALA content (related to amount of soluble protein) was signdicantly elevated in mercury-exposed oysters, in both the field and the laboratory. Sirmlar differences were observed for environmental samples of cockles Cerastoderrna edule (L ) , mussels Mytilus edulis (L.) and periwinkles L~ttorina littorea (L.) from the Cherninova slte and from uncontaminated samples. Possible cause-effect of the mercury-related Increase of ALA In molluscs is discussed.

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“…and S-Iactoylglutathione were purchased from Sigma Chemical Co., St. Louis, MO. 4,S-Dioxovalerate was prepared from 3,S-dibromolevulinate, which was also from Sigma, by the method of Varticovski et al 4 ) L-Lactaldehyde was prepared from Lthreonine according to Huff and Rudney.5) Yeast extract, Bacto peptone and malt extract were from Nakarai Chemical Co., Ltd., Kyoto, Japan.…”

Section: Methodsmentioning

confidence: 99%

Metabolism of 2-Oxoaldehydes in Bacteria: Purification and Characterization of Methylglyoxal Reductase fromEscherichia coli

Saikusa

Rhee

Watanabe

et al. 1987

Agricultural and Biological Chemistry

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Biosynthesis of porphyrin precursors: Kinetic studies on mammalian l-alanine: γ,δ-Dioxovaleric acid aminotransferase

Cited by 14 publications

References 13 publications

Biosynthesis of 5-aminolevulinic acid and heme from 4,5-dioxovalerate in the rat.

Biosynthesis of 5-aminolevulinic acid and heme from 4,5-dioxovalerate in the rat.

Effects of mercury on physiological condition and content of the biomarker ALA in the oyster Ostrea edulis

Metabolism of 2-Oxoaldehydes in Bacteria: Purification and Characterization of Methylglyoxal Reductase fromEscherichia coli

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