Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.170
Description:2-(omega-methylthio)alkylmalate dehydratase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.170
BRENDA Enzyme Link: BRENDA 4.2.1.170
KEGG Enzyme Link: KEGG4.2.1.170
BioCyc Enzyme Link: BioCyc 4.2.1.170
ExPASy Enzyme Link: ExPASy4.2.1.170
EC2PDB Enzyme Link: EC2PDB 4.2.1.170
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.170
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.170
IntEnz Enzyme Link: IntEnz 4.2.1.170
MEDLINE Enzyme Link: MEDLINE 4.2.1.170
MSA:

4.2.1.170;

Phylogenetic Tree:

4.2.1.170;

Uniprot:
M-CSA:
RHEA:50632 a 2-(omega-methylsulfanyl)alkylmalate = a 2-(omega-methylsulfanyl)alkylmaleate + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:5]-[*:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:5]-[*:6].[OH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.Knill T, Reichelt M, Paetz C, Gershenzon J, Binder S2009 Oct19597944

RHEA:50636 a 3-(omega-methylsulfanyl)alkylmalate = a 2-(omega-methylsulfanyl)alkylmaleate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:4]-[*:5].[OH2;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.Knill T, Reichelt M, Paetz C, Gershenzon J, Binder S2009 Oct19597944

RHEA:50648 2-(2-methylsulfanyl)ethylmalate = 2-(2-methylsulfanyl)ethylmaleate + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:5]-[*:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:5]-[*:6].[OH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.Knill T, Reichelt M, Paetz C, Gershenzon J, Binder S2009 Oct19597944

RHEA:50652 2-(3-methylsulfanyl)propylmalate = 2-(2-methylsulfanyl)propylmaleate + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:5]-[*:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:5]-[*:6].[OH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.Knill T, Reichelt M, Paetz C, Gershenzon J, Binder S2009 Oct19597944

RHEA:50656 3-(2-methylsulfanyl)ethylmalate = 2-(2-methylsulfanyl)ethylmaleate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:4]-[*:5].[OH2;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.Knill T, Reichelt M, Paetz C, Gershenzon J, Binder S2009 Oct19597944

RHEA:50660 3-(3-methylsulfanyl)propylmalate = 2-(2-methylsulfanyl)propylmaleate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:4]-[*:5].[OH2;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.Knill T, Reichelt M, Paetz C, Gershenzon J, Binder S2009 Oct19597944