
Browsing Pathways
Showing 495681 -
495690 of 605359 pathways
PathBank ID | Pathway Name and Description | Pathway Class | Chemical Compounds | Proteins |
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SMP0486449 |
N-Acetylneuraminate, N-Acetylmannosamine, and N-Acetylglucosamine DegradationEscherichia coli W
The degradation of N-acetylneuraminate begins with its incorporation into the cytosol through a hydrogen symporter. Once inside the cytosol it is degraded by a N-acetylneuraminate lyase resulting in a release of a pyruvic acid and N-acetymannosamine. The latter compound is phosphorylated by an ATP driven N-Acetylmannosamine kinase resulting in the release of an ADP, a hydrogen ion and a N-Acetyl-D-mannosamine 6-phosphate. This phosphorylated compound is then metabolized by a putative N-acetylmannosamine-6-phosphate 2-epimerase resulting in the release of a N-Acetyl-D-glucosamine 6-phosphate. This compound is then deacetylated through a N-acetylglucosamine-6-phosphate deacetylase resulting in the release of an Acetic acid and a glucosamine 6-phosphate This compound can then be deaminated through a glucosamine-6-phosphate deaminase resulting in the release of an ammonium and a beta-D-fructofuranose 6-phosphate which can then be incorporated into the glycolysis pathway.
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Metabolite
Metabolic
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SMP0486481 |
Spermidine Biosynthesis IEscherichia coli IHE3034
Spermidine is formed from decarboxy-SAM and putrescine by catalyzing spermidine synthase (also knowns as polyamine aminopropyltransferase). The source of putrescine is transported from outside of cell by putrescine/spermidine ABC transporter. Decarboxy-SAM comes from S-Adenosylmethionine with catalyzation of adenosylmethionine decarboxylase and cofactors: pyruvic acid and magnesium. The other product of the aminopropyltransferase reaction is S-methyl-5'-thioadenosine (MTA), which can be recycled back to L-methionine in many organisms, but not in E. coli. Inhibition of E. coli adenosylmethionine decarboxylase by spermidine appears to be the most significant regulator of polyamine biosynthesis, probably limiting it when the intracellular spermidine concentration becomes excessive. In E. coli most intracellular spermidine is bound to nucleic acids and phospholipids. (EcoCyc)
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Metabolite
Metabolic
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SMP0645939 |
Guanine and Guanosine SalvageBacteroides eggerthii 1_2_48FAA
Guanosine can be converted into guanine through a phosphate driven guanosine phosphorylase resulting in the release of an alpha-D-ribose 1 phosphate and a guanine. This compound in turn reacts with a PRPP through a guanine phosphoribosyltransferase resulting in the release of a pyrophosphate and a GMP.
Guanosine can also react with and ATP driven guanosine kinase resulting in the release of an ADP, s hydrogen ion and a GMP
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Metabolite
Metabolic
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SMP0486704 |
Guanine and Guanosine SalvageBacteroides oleiciplenus YIT 12058
Guanosine can be converted into guanine through a phosphate driven guanosine phosphorylase resulting in the release of an alpha-D-ribose 1 phosphate and a guanine. This compound in turn reacts with a PRPP through a guanine phosphoribosyltransferase resulting in the release of a pyrophosphate and a GMP.
Guanosine can also react with and ATP driven guanosine kinase resulting in the release of an ADP, s hydrogen ion and a GMP
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Metabolite
Metabolic
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SMP0645937 |
Guanine and Guanosine SalvageStreptococcus pneumoniae P1031
Guanosine can be converted into guanine through a phosphate driven guanosine phosphorylase resulting in the release of an alpha-D-ribose 1 phosphate and a guanine. This compound in turn reacts with a PRPP through a guanine phosphoribosyltransferase resulting in the release of a pyrophosphate and a GMP.
Guanosine can also react with and ATP driven guanosine kinase resulting in the release of an ADP, s hydrogen ion and a GMP
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Metabolite
Metabolic
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SMP0486640 |
Citrate Lyase ActivationBacteroides eggerthii DSM 20697
The citrate lyase activation starts with a 3-dephospho-CoA reacting with ATP and a hydrogen ion through a triphosphoribosyl-dephospho-CoA synthase resulting in a adenine and a 2'-(5'-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA. The latter compound in turn reacts with with a citrate lyase acyl-carrier protein through a apo-citrate lyase phosphoribosyl-dephospho-CoA transferase resulting in the release of a pyrophosphate and a hydrogen ion and a holo citrate lyase acyl-carrier protein.This protein complex can either react with a hydrogen ion and a acetate resulting in the release of a water and an acetyl-holo citrate lyase acyl-carrier protein.
The holo acyl-carrier protein creacts with an ATP and an acetate through a citrate lyase synthase resulting in the release of an AMP, a pyrophosphate and an acetyl-holo citrate lyase acyl-ccarrier protein.
The holo citrate lyase acyl-carrier protein can also interact with an S-acetyl phosphopantethiene resulting in the release of a 4-phosphopantethiene and an acetyl-holo citrate lyase acyl-carrier protein.
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Metabolite
Metabolic
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SMP0486676 |
Sedoheptulose Bisphosphate BypassBacteroides eggerthii DSM 20697
Sedoheptulose bisphospate bypass pathway demonstrates a series of reaction that form D-Erythrose 4-phosphate for pentose phosphate pathway and glycerone phosphate for glycolysis and pyruvate dehydrogenase pathway. D-Sedoheptulose 7-phosphate is obtained from pentose phosphate pathway, which later converted to sedoheptulose 1,7-bisphosphate via 6-phosphofructokinase-1. Fructose-bisphosphate aldolase class 2 catalyzes sedoheptulose 1,7-bisphosphate to form D-Erythrose 4-phosphate and pyruvate dehydrogenase.
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Metabolite
Metabolic
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SMP0645936 |
Sedoheptulose Bisphosphate BypassSpirosoma linguale DSM 74
Sedoheptulose bisphospate bypass pathway demonstrates a series of reaction that form D-Erythrose 4-phosphate for pentose phosphate pathway and glycerone phosphate for glycolysis and pyruvate dehydrogenase pathway. D-Sedoheptulose 7-phosphate is obtained from pentose phosphate pathway, which later converted to sedoheptulose 1,7-bisphosphate via 6-phosphofructokinase-1. Fructose-bisphosphate aldolase class 2 catalyzes sedoheptulose 1,7-bisphosphate to form D-Erythrose 4-phosphate and pyruvate dehydrogenase.
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Metabolite
Metabolic
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SMP0666337![]() |
Cardiolipin Biosynthesis CL(13:0/14:0/21:0/a-25:0)Rattus norvegicus
Cardiolipin (CL) is an important component of the inner mitochondrial membrane where it constitutes about 20% of the total lipid composition. It is essential for the optimal function of numerous enzymes that are involved in mitochondrial energy metabolism (Wikipedia). Cardiolipin biosynthesis occurs mainly in the mitochondria, but there also exists an alternative synthesis route for CDP-diacylglycerol that takes place in the endoplasmic reticulum. This second route may supplement this pathway. All membrane-localized enzymes are coloured dark green in the image. First, dihydroxyacetone phosphate (or glycerone phosphate) from glycolysis is used by the cytosolic enzyme glycerol-3-phosphate dehydrogenase [NAD(+)] to synthesize sn-glycerol 3-phosphate. Second, the mitochondrial outer membrane enzyme glycerol-3-phosphate acyltransferase esterifies an acyl-group to the sn-1 position of sn-glycerol 3-phosphate to form 1-acyl-sn-glycerol 3-phosphate (lysophosphatidic acid or LPA). Third, the enzyme 1-acyl-sn-glycerol-3-phosphate acyltransferase converts LPA into phosphatidic acid (PA or 1,2-diacyl-sn-glycerol 3-phosphate) by esterifying an acyl-group to the sn-2 position of the glycerol backbone. PA is then transferred to the inner mitochondrial membrane to continue cardiolipin synthesis. Fourth, magnesium-dependent phosphatidate cytidylyltransferase catalyzes the conversion of PA into CDP-diacylglycerol. Fifth, CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase synthesizes phosphatidylglycerophosphate (PGP). Sixth, phosphatidylglycerophosphatase and protein-tyrosine phosphatase dephosphorylates PGP to form phosphatidylglycerol (PG). Last, cardiolipin synthase catalyzes the synthesis of cardiolipin by transferring a phosphatidyl group from a second CDP-diacylglycerol to PG. It requires a divalent metal cation cofactor.
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Metabolite
Metabolic
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SMP0486657 |
O-Antigen Building Blocks BiosynthesisBacteroides eggerthii 1_2_48FAA
Lipopolysaccharide (LPS) is a major component of outer membrane which is consisted of lipid A-core (oligosaccharide) on both inner and outer region and O-antigen (known as distal repeating unit with four sugars: N-acetylglucosamine, glucose, rhamnose and galactose). O-antigen is part of three domains of LPS, which is attached to lipid A-core; however, O-antigen and lipid A-core are synthesized separately. In this pathway, synthesis of three of O-antigen sugars is demonstrated. UDP-α-D-galactose is converted to UDP-D-Galacto-1,4-furanose by facilitation of UDP-galactopyranose mutase. dTTP glucose-1-phosphate is derivatized to dTDP-rhamnose. Fructose-6-phosphate gains an amino group, incorporates an acetate moiety and then acquires a nucleoside diphosphate resulting in UDP-N-acetyl-D-glucosamine.
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Metabolic
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Showing 495681 -
495690 of 498628 pathways