4.1.2.13: fructose-bisphosphate aldolase
This is an abbreviated version!
For detailed information about fructose-bisphosphate aldolase, go to the full flat file.
Word Map on EC 4.1.2.13
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4.1.2.13
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creatine
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phosphofructokinase
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enolase
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hexokinase
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isozyme
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isoenzymes
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dihydroxyacetone
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glucose-6-phosphate
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erythrocyte
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phosphoglycerate
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aminotransferase
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albumin
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transaminase
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malate
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intolerance
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gapdh
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hereditary
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muscular
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phosphokinase
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glycogen
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pentose
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myopathy
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plasmodium
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gluconeogenesis
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schiff
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falciparum
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transketolase
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phosphoglucomutase
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purkinje
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dermatomyositis
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mutase
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phosphoglucose
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entner-doudoroff
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dhap
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myositis
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6-phosphogluconate
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gluconeogenic
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calvin
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myoglobin
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myalgia
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fructose-1,6-bisphosphatase
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tpi
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rhabdomyolysis
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polymyositis
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fbpase
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fructokinase
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medicine
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electromyography
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glycosomal
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parasagittal
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glutamic-oxalacetic
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molecular biology
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drug development
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diagnostics
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food industry
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agriculture
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synthesis
- 4.1.2.13
- creatine
-
phosphofructokinase
- enolase
- hexokinase
- isozyme
- isoenzymes
- dihydroxyacetone
- glucose-6-phosphate
- erythrocyte
- phosphoglycerate
- aminotransferase
- albumin
- transaminase
- malate
- intolerance
- gapdh
- hereditary
- muscular
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phosphokinase
- glycogen
- pentose
- myopathy
- plasmodium
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gluconeogenesis
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schiff
- falciparum
- transketolase
- phosphoglucomutase
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purkinje
- dermatomyositis
- mutase
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phosphoglucose
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entner-doudoroff
- dhap
- myositis
- 6-phosphogluconate
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gluconeogenic
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calvin
- myoglobin
- myalgia
- fructose-1,6-bisphosphatase
- tpi
- rhabdomyolysis
- polymyositis
- fbpase
- fructokinase
- medicine
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electromyography
- glycosomal
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parasagittal
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glutamic-oxalacetic
- molecular biology
- drug development
- diagnostics
- food industry
- agriculture
- synthesis
Reaction
Synonyms
1,6-Diphosphofructose aldolase, 37 kDa major allergen, 41 kDa antigen, ALD, ALDC, aldoA, Aldob, aldolase, aldolase A, aldolase B, aldolase C, aldolase, fructose diphosphate, ALDP, bifunctional fructose-1,6-bisphosphate aldolase/phosphatase, Brain-type aldolase, Ca-FBA-II, CE1, CE2, class I Fba, class I fructose 1,6-bisphosphate aldolase, class I fructose bisphosphate aldolase, class I fructose-1,6-bisphosphate aldolase, class I muscle fructose bis-phosphate aldolase, class II aldolase, class II FBA, class II FBP aldolase, class II fructose 1,6-bisphosphate aldolase, class II fructose bisphosphate aldolase, class II fructose-1,6-bisphosphate aldolase, class IIa fructose 1,6-bisphosphate aldolase, class IIb fructose 1,6-bisphosphate aldolase, ClassII FBP-aldolase, CoFBA1, CoFBA2, CoFBA3, CoFBA4, D-fructose-1,6-bisphosphate aldolase, D-fructose-1,6-bisphosphate D-glyceraldehyde-3-P-lyase, D-fructose-6-phosphate aldolase, Diphosphofructose aldolase, DLF, EC 4.1.2.7, F1,6-P2 aldolase, F1,6P2 aldolase, F16BP aldolase, FBA, FBA class II, FBA-II, Fba1, Fba1p, Fba2, FBA7, FbaA, FbaB, FbaC, FBAld, FbaP, FBP aldolase, FBP aldolase/phosphatase, FBP-aldolase, FBPA, FBPA I, FBPA-1, FBPA/P, FDP aldolase, FPA, Fru-1,6-P2 aldolase, Fru-P2A, Fructoaldolase, fructose 1,6 bisphosphate aldolase, fructose 1,6-bisphosphatase/aldolase, Fructose 1,6-bisphosphate aldolase, fructose 1,6-bisphosphate aldolase/phosphatase, Fructose 1,6-diphosphate aldolase, Fructose 1-monophosphate aldolase, Fructose 1-phosphate aldolase, fructose bis-phosphate aldolase, Fructose bisphosphate aldolase, Fructose diphosphate aldolase, fructose-1,6-biphosphate aldolase, fructose-1,6-bisphosphate (FBP) aldolase/phosphatase, fructose-1,6-bisphosphate aldolase, fructose-1,6-bisphosphate aldolase A, fructose-1,6-bisphosphate aldolase B, fructose-1,6-bisphosphate aldolase class II, fructose-1,6-bisphosphate aldolase/phosphatase, fructose-1,6-bisphosphate muscle aldolase, Fructose-1,6-bisphosphate triosephosphate-lyase, fructose-bisphosphate aldolase, fructose-bisphosphate aldolase A, FSA, fuculose aldolase, heat-induced protein 44, HIP44, IgE-binding allergen, ketose 1-phosphate aldolase, Leishmania aldolase, Liver-type aldolase, MGA3_01355, MJ0400-His6, More, MtFBA, Muscle-type aldolase, Ov-fba-1, OvFBPA-1, Pcal_0111, Phosphofructoaldolase, SMALDO, SSO0286, STK_03180, TgALD1, Tneu_0133, TnFBPAP, Tt-FBPA, zerebrin II, zymohexase
ECTree
4.1.2.13 fructose-bisphosphate aldolaseAdvanced search results
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General Information on EC 4.1.2.13 - fructose-bisphosphate aldolase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
potential target for drug development against pathogenic bacteria
drug target
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
drug target
the enzyme is an attractive targets for the discovery of drugs to combat invasive fungal infection, because it is absent in animals and higher plants. It is a promising target for the discovery of drugs against azole-resistant fungal pathogens in the future
drug target
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potential target for drug development against pathogenic bacteria
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drug target
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the enzyme is an attractive targets for the discovery of drugs to combat invasive fungal infection, because it is absent in animals and higher plants. It is a promising target for the discovery of drugs against azole-resistant fungal pathogens in the future
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drug target
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the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
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evolution
the archaeal enzyme belongs to the class V of fructose-1,6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
Vibrio anguillarum MVM425
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the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
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evolution
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the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
evolution
-
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
evolution
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the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
evolution
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the archaeal enzyme belongs to the class V of fructose-1,6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
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evolution
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the archaeal enzyme belongs to the class V of fructose-1,6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
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evolution
Aeromonas hydrophila ATCC 7699
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the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
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evolution
Pyrobaculum calidifontis JGM 11548
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the archaeal enzyme belongs to the class V of fructose-1,6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
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malfunction
deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated
malfunction
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decreasing fructose-1,6-bisphosphate aldolase activity reduces plant growth and tolerance to chilling stress in tomato seedlings
malfunction
enzyme inactivation impairs virulence and increases resistance to oxidative stress
malfunction
enzyme knockdown stops cell cycle progression and enhances apoptosis due to rapid accumulation of reactive oxygen species
malfunction
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knockdown of fructose-1,6-bisphosphate aldolases activates AMP-activated protein kinase even in cells with abundant glucose, while the catalysis-defective D34S aldolase mutant, which still binds fructose-1,6-bisphosphate, blocks AMP-activated protein kinase activation
malfunction
knockdown of the enzyme stops cell cycle progression and enhances apoptosis due to rapid accumulation of reactive oxygen species
malfunction
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the interference of SlFBA7 expression decreases the regeneration of ribulose-1,5-bisphosphate and the CO2 fixation in the Calvin-Benson cycle and leads to reduced growth and development of tomato seedlings. Inhibition of SlFBA7 expression and activity of fructose-1,6-bisphosphate aldolase decreases the levels of net photosynthetic rate and increases the H2O2 and O2(·-) accumulation in the RNAi transgenic tomato seedlings under chilling stress
malfunction
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enzyme inactivation impairs virulence and increases resistance to oxidative stress
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malfunction
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deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated
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metabolism
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chloroplastic fructose 1,6-bisphosphate aldolase isoforms are methylated by protein-lysine methyltransferase LSMT. Trimethylation occurs at a conserved lysyl residue located close to the C terminus. Trimethylation does not modify the kinetic properties and tetrameric organization of the aldolases in vitro
metabolism
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the enzyme is a sensor of glucose availability that regulates AMP-activated protein kinase
metabolism
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the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
metabolism
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the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
metabolism
metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes
metabolism
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the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
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metabolism
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metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes
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physiological function
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ALDOA is involved in keratinocyte migration following the induction of lamellipodia formation, and ALDOA-related migration is enhanced by epidermal growth factor
physiological function
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FBA is required for optimal adhesion of meningococci to human cells
physiological function
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the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
gene product is required for the growth of Mycobacterium tuberculosis on gluconeogenetic substrates and in glucose-containing medium
physiological function
isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene
physiological function
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mutagenesis in a unique fbaB gene of Xanthomonas oryzae pv. oryzicola, the causal agent of rice bacterial leaf streak, leads the pathogen unable to use pyruvate and malate for growth and delays its growth when fructose is used as the sole carbon source, but also reduces extracellular polysaccharide production and impairs bacterial virulence and growth in rice. The expression of hrpG and hrpX encoding a type-III secretion system is repressed and the transcripts of hrcC, hrpE and hpa3 are enhanced when fbaB is deleted
physiological function
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose
physiological function
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the enzyme is involved in glycogen catabolism
physiological function
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the overproduction of fructose bisphosphate aldolase Fba1 enables overcoming of a severe growth defect caused by a missense mutation rpc128-1007 in a gene encoding the C128 protein, the second largest subunit of the RNA polymerase III complex. The suppression of the growth phenotype by Fba1 is accompanied by enhanced de novo tRNA transcription in rpc128-1007 cells. Overproduction of an inactive aldolase mutant still suppresses the rpc128-1007 phenotype, and Fba1 interacts with the RNA polymerase III complex and plays a role in control of tRNA transcription
physiological function
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the seed germination and root elongation of knock-out plants exhibits sensitivity to abscisic acid and salt stress. Gene is able to complement the salt-sensitive phenotype of a calcineurin-deficient yeast mutant
physiological function
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transgenic Nicotiana tabacum L. cv Xanthi expressing Arabidopsis plastid aldolase shows 1.4-1.9fold higher aldolase activities than wild-type, associated with enhanced growth, culminating in increased biomass, particularly under high CO2 concentration where the increase reached 2.2fold relative to wild-type plants. This increase is associated with a 1.5fold elevation of photosynthetic CO2 fixation in the transgenic plants. Overexpression results in a decrease in 3-phosphoglycerate and an increase in ribulose 1,5-bisphosphate and its immediate precursors in the Calvin cycle
physiological function
enzyme expression is necessary for cancer cells to grow in hypoxic conditions
physiological function
the enzyme is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, there is a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
physiological function
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the enzyme is required for optimal adhesion to human cells
physiological function
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the enzyme regulates growth and chilling tolerance of tomato seedlings
physiological function
fructose-1,6-bisphosphate aldolase B catalyses the reversible reaction of glyceraldehyde-3-phosphate (G3-P) and dihydroxyacetone phosphate (DHAP) to form fructose 1,6-bisphosphate and participates in both gluconeogenesis and glycolysis. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver fructose 1,6-bisphosphatase (FBPase-1) shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate. FBPase-1 guides the cellular localization of aldolase B
physiological function
CoFAD2 is directly involved in fatty acid metabolic pathway in the oilseeds
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
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conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. Fructose-1,6-bisphosphate aldolase is immunogenic in Streptococcus suis SS9
physiological function
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conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The enzyme from Mycobacterium tuberculosis binds human plasminogen
physiological function
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conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The enzyme from Neisseria meningitidis is dispensable for survival of, but required for optimal adhesion to human cells
physiological function
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conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The Pneumococcal enzyme is an immunogenic adhesin which binds Flamingo cadherin receptor
physiological function
during invasion of the apicomplexan parasite Toxoplasma gondii into host cells, the enzyme serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway
physiological function
fructose-1,6-bisphosphate aldolase (CoFBA) and stearoyl-ACP desaturase (CoSAD) gene expression is well-correlated with oil content in Camellia seeds
physiological function
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overproduction of the recombinant enzyme (msFBAld) in Escherichia coli results in increased tolerance towards salinity
physiological function
possible participation of the enzyme in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides
physiological function
the enzyme is a key regulator of hypoxic adaptation in colorectal cancer cells
physiological function
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the enzyme is a natural fructose-1,6-bisphosphate receptor that transmits the effects of glucose shortage to AMP-activated protein kinase via the v-ATPase-Ragulator-AXIN/LKB1 complex
physiological function
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the enzyme is involved in adhesion to host cells. It binds human plasminogen via its C-terminal lysine residue, whereas subterminal lysine residues are not involved
physiological function
the enzyme occupies a central position in glycolysis and gluconeogenesis pathways. Fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. Direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
physiological function
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the enzyme plays vital role in glycolysis and gluconeogenesis
physiological function
the enzyme positively regulates the activity of the glycolytic pathway and the epithelial-mesenchymal transition and is necessary for cell cycle progression. It is implicated in colorectal cancer proliferation, sphere formation, therapeutic resistance and invasion
physiological function
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possible participation of the enzyme in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides
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physiological function
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possible participation of the enzyme in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides
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physiological function
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the enzyme is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, there is a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
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physiological function
-
the enzyme occupies a central position in glycolysis and gluconeogenesis pathways. Fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. Direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
-
physiological function
Vibrio anguillarum MVM425
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conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
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physiological function
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conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. Fructose-1,6-bisphosphate aldolase is immunogenic in Streptococcus suis SS9
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physiological function
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fructose-1,6-bisphosphate aldolase B catalyses the reversible reaction of glyceraldehyde-3-phosphate (G3-P) and dihydroxyacetone phosphate (DHAP) to form fructose 1,6-bisphosphate and participates in both gluconeogenesis and glycolysis. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver fructose 1,6-bisphosphatase (FBPase-1) shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate. FBPase-1 guides the cellular localization of aldolase B
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physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The Pneumococcal enzyme is an immunogenic adhesin which binds Flamingo cadherin receptor
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
during invasion of the apicomplexan parasite Toxoplasma gondii into host cells, the enzyme serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway
-
physiological function
-
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose
-
physiological function
-
isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene
-
physiological function
Aeromonas hydrophila ATCC 7699
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conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
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additional information
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
additional information
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the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
additional information
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the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
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additional information
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the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
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additional information
Pyrobaculum calidifontis JGM 11548
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the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
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