4.2.1.36: homoaconitate hydratase
This is an abbreviated version!
For detailed information about homoaconitate hydratase, go to the full flat file.
Word Map on EC 4.2.1.36
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4.2.1.36
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alpha-aminoadipate
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homocitrate
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isopropylmalate
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auxotrophy
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homoisocitrate
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l-lysine
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lys4
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jannaschii
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saccharopine
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methanocaldococcus
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synthesis
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medicine
- 4.2.1.36
- alpha-aminoadipate
- homocitrate
- isopropylmalate
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auxotrophy
- homoisocitrate
- l-lysine
- lys4
- jannaschii
- saccharopine
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methanocaldococcus
- synthesis
- medicine
Reaction
Synonyms
2-hydroxy-3-carboxyadipate hydro-lyase, cis-Homoaconitase, HACN, HACNMj, Homoaconitase, Homoaconitate hydratase, Hydratase, homoaconitate, leuC, LYS4, lysF, MJ0499, MJ1271
ECTree
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Substrates Products
Substrates Products on EC 4.2.1.36 - homoaconitate hydratase
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REACTION DIAGRAM
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
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i.e. cis-homoaconitate, three different stereoisomeric substrate types, cis-homo1-aconitate, cis-homo2-aconitate, and cis-homo3-aconitate, in the reaction, overview
i.e. homoisocitrate, Arg26 of MJ1271 plays a key role in homoaconitate substrate recognition, while discriminating against the hydrophobic methyl or isopropyl gamma-chains of citraconate and 3-isopropylmalate. Catalytic Ser67 and Arg69 residues in the IMPI small subunit MJ1277 model are equivalent to Ser65 and Arg67 in MJ1271, but residues Val28-Tyr29 replace the polar Arg26-Thr27 residues in the flexible loop region between alpha2 and alpha3
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r
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
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(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
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r
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enzyme is involved in the L-Lys biosynthesis via 2-aminoadipate pathway
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2-Hydroxy-3-carboxyadipate
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evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea
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2-Hydroxy-3-carboxyadipate
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evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea
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2-Hydroxy-3-carboxyadipate
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enzyme is involved in the L-Lys biosynthesis via 2-aminoadipate pathway
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2-Hydroxy-3-carboxyadipate
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enzyme of the homocitrate pathway
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2-Hydroxy-3-carboxyadipate
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evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea
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?
2-Hydroxy-3-carboxyadipate
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enzyme of the lysine biosynthetic pathway
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but-1-ene-1,2,4-tricarboxylate + H2O
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2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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?
2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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?
2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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?
2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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?
2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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-
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?
2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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-
-
?
2-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylate + H2O
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?
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HACNMj is specific for cis-unsaturated tricarboxylates, while isopropylmalate isomerase, IPMIMj, recognizes cis-unsaturated dicarboxylates, substrate specificity determinants of homologous IPMI and HACN proteins from Methanocaldococcus jannaschii from a structural model show characteristic residues in a flexible loop region between R2 and R3 that distinguish HACN from IPMI and aconitase proteins, overview
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