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Pathways

PathWhiz ID Pathway Meta Data

PW123548

Pw123548 View Pathway
metabolic

1,6-Anhydro-N-acetylmuramic Acid Recycling

Pseudomonas aeruginosa
Most bacteria, including Escherichia coli, are composed of murein which protects and stabilizes the cell wall. Over half of the murein is broken down by Escherichia coli and recycled for the next generation. The main muropeptide is GlcNAc-anhydro-N-acetylmuramic acid (anhMurNAc)-l-Ala-γ-d-Glu-meso-Dap-d-Ala which enters the cytoplasm by AmpG protein. The peptide is then released from the muropeptide. 1,6-Anhydro-N-acetylmuramic acid (anhMurNAc) is recycled by its conversion to N-acetylglucosamine-phosphate (GlcNAc-P). The sugar is phosphorylated by anhydro-N-acetylmuramic acid kinase (AnmK) to produce MurNAc-P. Etherase cleaves MurNAc-P to produce N-acetyl-D-glucosamine 6-phosphate. The product can undergo further degradation or be recycled into peptidoglycan monomers. The pathway's final product is a peptidoglycan biosynthesis precursor, UDP-N-acetyl-α-D-muramate. The enzyme muropeptide ligase (mpl), attaches the recovered Ala-Glu-DAP tripeptide to the precursor UDP-N-acetyl-α-D-muramate to return to the peptide to the peptidoglycan biosynthetic pathway to synthesize the cell wall.

PW126201

Pw126201 View Pathway
metabolic

1-Methylhistidine Metabolism

Homo sapiens
Methylhistidine is a modified amino acid that is produced in myocytes during the methylation of actin and myosin. It is also formed from the methylation of L-histidine, which takes the methyl group from S-adenosylmethionine and forms S-adenosylhomocysteine as a byproduct. After its formation in the myocytes, methylhistidine enters the blood stream and travels to the kidneys, where it is excreted in the urine. Methylhistidine is present in the blood and urine in higher concentrations after skeletal muscle protein breakdown, which can occur due to disease or injury. Because of this, it can be used to judge how much muscle breakdown is occurring. Methylhistidine levels are also affected by diet, and may differ between vegetarian diets and those containing meats.

PW126354

Pw126354 View Pathway
metabolic

1-Methylhistidine synthesis via METTL9-catalyzed methylation

Homo sapiens

PW146354

Pw146354 View Pathway
drug action

1-Palmitoyl-2-oleoyl-sn-glycero-3-(phospho-rac-(1-glycerol)) Drug Metabolism Action Pathway

Homo sapiens

PW064700

Pw064700 View Pathway
signaling

1.      Barrier

Homo sapiens

PW000551

Pw000551 View Pathway
disease

11-beta-Hydroxylase Deficiency (CYP11B1)

Homo sapiens
11-beta-Hydroxylase Deficiency, also called congenital adrenal hyperplasia (CAH), is an autosomal recessive disorder and caused by a defective 11-beta-hydroxylase. 11-beta-hydroxylase catalyzes the conversion of cortexolone into cortisol which is useful for maintaining blood sugar levels and suppressing inflammation. This disorder is characterized by a large accumulation of cortexolone in the endoplasmic reticulum (ER). Symptoms of the disorder include abnormality of hair growth rate and menstrual cycle. It is estimated that 11-beta-hydroxylase deficiency affects 1 in 100,000 to 200,000 newborns.

PW122119

Pw122119 View Pathway
disease

11-beta-Hydroxylase Deficiency (CYP11B1)

Rattus norvegicus
11-beta-Hydroxylase Deficiency, also called congenital adrenal hyperplasia (CAH), is an autosomal recessive disorder and caused by a defective 11-beta-hydroxylase. 11-beta-hydroxylase catalyzes the conversion of cortexolone into cortisol which is useful for maintaining blood sugar levels and suppressing inflammation. This disorder is characterized by a large accumulation of cortexolone in the endoplasmic reticulum (ER). Symptoms of the disorder include abnormality of hair growth rate and menstrual cycle. It is estimated that 11-beta-hydroxylase deficiency affects 1 in 100,000 to 200,000 newborns.

PW121895

Pw121895 View Pathway
disease

11-beta-Hydroxylase Deficiency (CYP11B1)

Mus musculus
11-beta-Hydroxylase Deficiency, also called congenital adrenal hyperplasia (CAH), is an autosomal recessive disorder and caused by a defective 11-beta-hydroxylase. 11-beta-hydroxylase catalyzes the conversion of cortexolone into cortisol which is useful for maintaining blood sugar levels and suppressing inflammation. This disorder is characterized by a large accumulation of cortexolone in the endoplasmic reticulum (ER). Symptoms of the disorder include abnormality of hair growth rate and menstrual cycle. It is estimated that 11-beta-hydroxylase deficiency affects 1 in 100,000 to 200,000 newborns.

PW127367

Pw127367 View Pathway
disease

11-beta-Hydroxylase Deficiency (CYP11B1)

Homo sapiens
11-beta-Hydroxylase Deficiency, also called congenital adrenal hyperplasia (CAH), is an autosomal recessive disorder and caused by a defective 11-beta-hydroxylase. 11-beta-hydroxylase catalyzes the conversion of cortexolone into cortisol which is useful for maintaining blood sugar levels and suppressing inflammation. This disorder is characterized by a large accumulation of cortexolone in the endoplasmic reticulum (ER). Symptoms of the disorder include abnormality of hair growth rate and menstrual cycle. It is estimated that 11-beta-hydroxylase deficiency affects 1 in 100,000 to 200,000 newborns.

PW122336

Pw122336 View Pathway
metabolic

11-cis-3-Hydroxyretinal Biosynthesis

Drosophila melanogaster
(3S)-11-cis-3-hydroxyretinal is one of three chromophores, which then associate with rhodopsins. Specifically, this chromophore associates with the Rh1 rhodopsin, a blue/green sensitive visual pigment found in 6 of the 8 photoreceptor cells in Drosophila melanogaster. The production of this chromophore begins with zeaxanthin obtained from Drosophila’s dietary sources. This lipid is broken down into (3R)-11-cis-3-hydroxyretinal and (3R)-all-trans-3-hydroxyretinal by a carotenoid isomerooxygenase. The (3R)-cis-3-hydroxyretinal is then attached to a retinoid binding protein, and this complex goes on to be used in the visual cycle of the organism. However, (3R)-all-trans-3-hydroxyretinal must be further processed. It too binds to a retinoid binding protein that will remain unchanged through the rest of the reactions. First, this complex will have a hydrogen added by a photoreceptor dehydrogenase in order to form (3R)-all-trans-3-hydroxyretinol, and then a photoreceptor epimerase will invert its stereochemistry to form (3S)-all-trans-3-hydroxyretinol. From here, an unknown protein, an oxidoreductase that transposes C=C bonds, will form (3S)-11-cis-3-hydroxyretinol. Finally, another photoreceptor dehydrogenase removes a hydrogen from that complex, forming the final product, (3S)-11-cis-3-hydroxyretinal. This complex then joins (3R)-11-cis-3-hydroxyretinal in the visual cycle.