5-Aminolevulinic acid level and dye-decolorizing peroxidase expression regulate heme synthesis in Escherichia coli

2021 ◽  
Author(s):  
Chaoqun Feng ◽  
Mei Pan ◽  
Lei Tang
Keyword(s):  
Escherichia Coli ◽  
Acid Level ◽  
Aminolevulinic Acid ◽  
Heme Synthesis

scholarly journals Role of the hemA gene product and delta-aminolevulinic acid in regulation of Escherichia coli heme synthesis.

1997 ◽  
Vol 179 (14) ◽  
pp. 4583-4590 ◽  
Author(s):  
E Verderber ◽  
L J Lucast ◽  
J A Van Dehy ◽  
P Cozart ◽  
J B Etter ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Aminolevulinic Acid ◽  
Heme Synthesis ◽  
Hema Gene

Stable and Efficient Biosynthesis of 5-Aminolevulinic Acid Using Plasmid-Free Escherichia coli

2019 ◽  
Vol 67 (5) ◽  
pp. 1478-1483 ◽  
Author(s):  
Zhiyong Cui ◽  
Zhennan Jiang ◽  
Jinhong Zhang ◽  
Huihui Zheng ◽  
Xin Jiang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Aminolevulinic Acid

scholarly journals The Utilization of Protoporphyrin 9 in Heme Synthesis

Blood ◽  
1959 ◽  
Vol 14 (4) ◽  
pp. 476-485 ◽  
Author(s):  
MOISES GRINSTEIN ◽  
ROBIN M. BANNERMAN ◽  
CARL V. MOORE
Keyword(s):  
Cell Membrane ◽  
Human Blood ◽  
Biosynthetic Pathway ◽  
Aminolevulinic Acid ◽  
Thalassemia Major ◽  
Heme Synthesis ◽  
Equivalent Quantity ◽  
Chicken Erythrocytes

Abstract The experiments described in this communication demonstrate that C14-tagged protoporphyrin 9 can be incorporated into the heme during the biosynthesis of hemoglobin. 1. In vitro observations: (a) C14 protoporphyrin 9 was found to be incorporated into heme by hemolysates of chicken and human blood incubated at 37 C. The degree of incorporation by washed chicken erythrocytes was less, presumably because the protoporphyrin was not readily transferred across the cell membrane. Incorporation by hemolysates was inhibited completely at 1 x 10-2 M KCN at 4 C., markedly by 1 x 10-2 M KCN at 37 C. and partially by 1 x 10-3 M Pb at 37 C. (b) The degree of incorporation was reduced by the addition of an equivalent quantity of delta-aminolevulinic acid. Furthermore, the incorporation of glycine-2-C14 into heme was reduced by the addition of an equivalent quantity of protoporphyrin 9. 2. In vivo observations: Intravenously administered C14 protoporphyrin was incorporated into the circulating hemoglobin of two rabbits with a phenylhydrazine-induced hemolytic anemia. These observations provide support for the view that protoporphyrin 9 itself is a true direct precursor of hemoglobin, in the biosynthetic pathway between porphobilinogen and heme. Comparative studies of rates of incorporation of C14 protoporphyrin 9 and its precursors into heme in vitro may provide a useful tool for the study of heme synthesis in normal and pathologic conditions. For instance, it was shown that hemolysates from the blood of patients with thalassemia major, with poor iron and glycine utilization, rapidly incorporated the tagged protoporphyrin into heme.

scholarly journals delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli.

1991 ◽  
Vol 173 (1) ◽  
pp. 94-100 ◽  
Author(s):  
G P O'Neill ◽  
S Thorbjarnardóttir ◽  
U Michelsen ◽  
S Pálsson ◽  
D Söll ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Aminolevulinic Acid ◽  
Acid Dehydratase

scholarly journals Iron distribution in Belgrade rat reticulocytes after inhibition of heme synthesis with succinylacetone

Blood ◽  
1993 ◽  
Vol 81 (12) ◽  
pp. 3414-3421 ◽  
Author(s):  
LM Garrick ◽  
K Gniecko ◽  
Y Liu ◽  
DS Cohan ◽  
JA Grasso ◽  
...  
Keyword(s):  
Iron Uptake ◽  
Iron Transport ◽  
Aminolevulinic Acid ◽  
Specific Inhibitor ◽  
Hypochromic Anemia ◽  
Endocytic Vesicle ◽  
Heme Synthesis ◽  
Diferric Transferrin ◽  
Rat Reticulocytes ◽  
Insight Into

Abstract We have used succinylacetone (4,6-dioxoheptanoic acid), a specific inhibitor of delta-aminolevulinic acid dehydrase, to gain insight into the defect in iron metabolism in the Belgrade anemia. The Belgrade rat has an inherited microcytic, hypochromic anemia associated with poor iron uptake into developing erythroid cells. Succinylacetone inhibits heme synthesis, leading to nonheme iron accumulation in mitochondria and cytosol of normal reticulocytes. When succinylacetone is used to inhibit Belgrade heme synthesis, iron from diferric transferrin does not accumulate in the stromal fraction that contains mitochondria, nor does 59Fe accumulate in the nonheme cytosolic fraction. Hence, the defect in the Belgrade rat reticulocyte occurs in the endocytic vesicle or in a step subsequent to iron transit from the vesicle but before the nonheme cytosolic or mitochondrial iron fractions. Therefore, the mutation affects either the release of iron from transferrin or iron transport from the vesicle to the mitochondrion.

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