Information on EC 4.2.1.9 - dihydroxy-acid dehydratase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
4.2.1.9
-
RECOMMENDED NAME
GeneOntology No.
dihydroxy-acid dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
show the reaction diagram
-
-
-
-
2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
show the reaction diagram
stereochemistry, elimination and protonation steps are stereospecific, enol-keto conversion takes place with proton addition at C-3 to the same face of the enol as that of the departing hydroxy-group
-
2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
show the reaction diagram
polar but concerted elimination mechanism which should proceed through an anti transition state
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
isoleucine biosynthesis I (from threonine)
-
isoleucine biosynthesis II
-
isoleucine biosynthesis III
-
isoleucine biosynthesis IV
-
Metabolic pathways
-
Pantothenate and CoA biosynthesis
-
pyruvate fermentation to isobutanol (engineered)
-
valine biosynthesis
-
Valine, leucine and isoleucine biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
2,3-dihydroxy-3-methylbutanoate hydro-lyase (3-methyl-2-oxobutanoate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2,3-dihydroxy acid hydrolyase
-
-
-
-
2,3-dihydroxyisovalerate dehydratase
-
-
-
-
acetohydroxyacid dehydratase
-
-
-
-
alpha,beta-dihydroxy acid dehydratase
-
-
-
-
alpha,beta-dihydroxyisovalerate dehydratase
-
-
-
-
DAD
-
-
-
-
dehydratase, dihydroxy acid
-
-
-
-
DHAD
-
-
-
-
dihydroxy acid dehydrase
-
-
-
-
dihydroxy acid dehydratase
-
-
-
-
dihydroxy acid dehydratase
-
-
dihydroxyacid dehydratase
-
-
-
-
dihydroxyacid dehydratase
-
-
dihydroxyacid dehydratase
Q8NQZ9
-
dihydroxyacid dehydratase
Q8NQZ9
-
-
dihydroxyacid dehydratase
-
-
dihydroxyacid dehydratase
-
-
VEG110
-
-
-
-
Vegetative protein 110
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-32-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 15150; wild type strain BD-413
-
-
Manually annotated by BRENDA team
Acinetobacter sp. 15150
strain 15150
-
-
Manually annotated by BRENDA team
Chromatium sp.
strain D
-
-
Manually annotated by BRENDA team
Chromatium sp. D
strain D
-
-
Manually annotated by BRENDA team
gene ilvD
Q8NQZ9
UniProt
Manually annotated by BRENDA team
gene ilvD, strain ilvNM13, ATCC 13032
-
-
Manually annotated by BRENDA team
CGSC strain 5073; K-12
-
-
Manually annotated by BRENDA team
gene Rv0189c or ilvD
-
-
Manually annotated by BRENDA team
wild type strain KJT 1960 and iv-mutant strain 332
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
dihydroxyacid dehydratase, a key enzyme involved in branched-chain amino acid biosynthesis, catalyses the synthesis of 2-oxoacids from dihydroxyacids
metabolism
-
DHAD is involved in the biosynthetic pathways of L-valine, L-isoleucine, L-leucine, and D-pantothenate, regulation, overview
metabolism
-
dihydroxyacid dehydratase, a key enzyme involved in branched-chain amino acid biosynthesis, catalyses the synthesis of 2-oxoacids from dihydroxyacids
metabolism
-
DHAD is involved in the biosynthetic pathways of L-valine, L-isoleucine, L-leucine, and D-pantothenate, regulation, overview
-
physiological function
-
Rv0189c has a role in the survival of Mycobacterium tuberculosis during normal and stress conditions
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-2,3-dihydroxy-3-ethylpentanoate
?
show the reaction diagram
-
20% of the activity with 2,3-dihydroxyisovalerate
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
-
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
-
no activity with 2S-2,3-dihydroxy-3-methylbutanoate, 2R-2,3-dihydroxy-3-methylbutanoate
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
Chromatium sp. D
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
2-oxoisovalerate + H2O
show the reaction diagram
Acinetobacter sp. 15150
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
3-methyl-2-oxobutanoate + H2O
show the reaction diagram
Q8NQZ9
-
i.e. 2-ketoisovalerate
-
?
2,3-dihydroxy-3-methylbutanoate
3-methyl-2-oxobutanoate + H2O
show the reaction diagram
-
-
i.e. 2-ketoisovalerate, i.e. alpha-ketoisovalerate
-
?
2,3-dihydroxy-3-methylbutanoate
3-methyl-2-oxobutanoate + H2O
show the reaction diagram
Q8NQZ9
-
i.e. 2-ketoisovalerate, i.e. alpha-ketoisovalerate
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
2R,3R-(2,3)-dihydroxy-3-methylpentanoate, at 45% of the activity with 2,3-dihydroxyisovalerate
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
2R,3S-2,3-dihydroxy-3-methylpentanoate, 2R,3R-2,3-dihydroxy-3-methylpentanoate
-
-
-
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
-
2R,3R-dihydroxy-3-methylpentanoate, 2R,3S-dihydroxy-3-methylpentanoate, no activity with isomers with 2S configuration
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
Chromatium sp. D
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
3-methyl-2-oxopentanoate + H2O
show the reaction diagram
Acinetobacter sp. 15150
-
-
-
?
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
involved in synthesis of Ile
-
-
-
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
2R,3R-(2,3)-dihydroxy-3-methylpentanoate
-
-
-
2,3-dihydroxy-3-methylvalerate
3-methyl-2-oxovalerate
show the reaction diagram
-
-
-
-
?
2,3-dihydroxy-isovalerate
2-oxoisovalerate
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybutanoate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
involved in biosynthesis of Val
-
-
-
2,3-dihydroxyisovalerate
2-oxovalerate + H2O
show the reaction diagram
-
IlvD, an iron-sulfur enzyme, catalyses the conversion from 2,3-dihydroxyisovalerate to 2-keto-isovalerate and is essential for the branchend-chain amino acid biosynthesis
-
-
?
3-cyclopropyl-2,3-dihydroxybutanoate
?
show the reaction diagram
-
-
-
-
-
D,L-2,3-dihydroxy-isovalerate
?
show the reaction diagram
-
-
-
-
?
D-arabonate
?
show the reaction diagram
-
-
-
-
?
D-erythronate
?
show the reaction diagram
-
-
-
-
?
D-fuconate
?
show the reaction diagram
-
-
-
-
?
D-Galacturonate
?
show the reaction diagram
-
-
-
-
?
D-gluconate
2-keto-3-deoxygluconate + H2O
show the reaction diagram
-
-
-
-
?
D-Glucuronate
?
show the reaction diagram
-
-
-
-
?
D-xylonate
?
show the reaction diagram
-
-
-
-
?
DL-2,3-dihydroxyisovalerate
2-oxo-isovalerate + H2O
show the reaction diagram
-
-
-
-
?
DL-2,3-dihydroxyisovalerate
?
show the reaction diagram
-
-
-
-
?
threo-2,3-dihydroxybutanoate
?
show the reaction diagram
-
at 45% of the activity with 2,3-dihydroxyisovalerate
-
-
?
L-threonate
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
third enzyme in the branched-chain amino acid biosynthetic pathway
-
-
-
additional information
?
-
-
dihydroxy-acid dehydratase is one of the key enzymes involved in the biosynthetic pathway of the branched chain amino acids
-
-
-
additional information
?
-
-
reaction product determination by formation of 2,4-dinitrophenylhydrazone from the keto acid product resulting in 2-ketoisovalerate-dinitrophenylhydrazone
-
-
-
additional information
?
-
Q8NQZ9
reaction product determination by formation of 2,4-dinitrophenylhydrazone from the keto acid product resulting in 2-ketoisovalerate-dinitrophenylhydrazone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxy-3-methylbutanoate
3-methyl-2-oxobutanoate + H2O
show the reaction diagram
Q8NQZ9
-
i.e. 2-ketoisovalerate
-
?
2,3-dihydroxy-3-methylbutanoate
3-methyl-2-oxobutanoate + H2O
show the reaction diagram
-
-
i.e. 2-ketoisovalerate
-
?
2,3-dihydroxy-3-methylbutanoate
3-methyl-2-oxobutanoate + H2O
show the reaction diagram
Q8NQZ9
-
i.e. 2-ketoisovalerate
-
?
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
involved in synthesis of Ile
-
-
-
2,3-dihydroxy-3-methylpentanoate
?
show the reaction diagram
-
2R,3R-(2,3)-dihydroxy-3-methylpentanoate
-
-
-
2,3-dihydroxy-3-methylvalerate
3-methyl-2-oxovalerate
show the reaction diagram
-
-
-
-
?
2,3-dihydroxy-isovalerate
2-oxoisovalerate
show the reaction diagram
-
-
-
-
?
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
-
-
-
-
2,3-dihydroxyisovalerate
?
show the reaction diagram
-
involved in biosynthesis of Val
-
-
-
2,3-dihydroxyisovalerate
2-oxovalerate + H2O
show the reaction diagram
-
IlvD, an iron-sulfur enzyme, catalyses the conversion from 2,3-dihydroxyisovalerate to 2-keto-isovalerate and is essential for the branchend-chain amino acid biosynthesis
-
-
?
DL-2,3-dihydroxyisovalerate
2-oxo-isovalerate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
third enzyme in the branched-chain amino acid biosynthetic pathway
-
-
-
additional information
?
-
-
dihydroxy-acid dehydratase is one of the key enzymes involved in the biosynthetic pathway of the branched chain amino acids
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activates
Co2+
-
divalent cation required. Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ are nearly equally effective
Fe2+
-
divalent metal ion required, Fe2+ is most effective
Fe2+
-
divalent cation required. Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ are nearly equally effective
Fe2+
-
the enzyme contains a [4Fe-4S] cluster
Iron
-
contains a catalytically active [2Fe-2S] cluster
Iron
-
contains a [4Fe-4S]2+,+ cluster which is essential for catalysis and unstable in the presence of O2 and O2-
Iron
-
contains a catalytically active [4Fe-4S] cluster
Iron
-
contains a catalytically active [4Fe-4S] cluster; studies on the synthesis of Fe-S cluster
Iron
-
an iron-sulfur enzyme, requires an intact [4Fe-4S] cluster
Mg2+
-
divalent metal ion required, less effective than Fe2+
Mg2+
-
required
Mg2+
-
required for maximal activity, maximal activity at 0.01 M
Mg2+
-
divalent cation required. Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ are nearly equally effective
Mn2+
-
divalent metal ion required, less effective than Fe2+
Mn2+
-
activates
Mn2+
-
divalent cation required. Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ are nearly equally effective
Mn2+
-
enhances activity
Ni2+
-
divalent cation required. Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ are nearly equally effective
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4,5,6-tetrahydroxyhexanoate
-
-
2,4,5-trihydroxypentanoate
-
-
2,4-dihydroxybutanoate
-
-
2-mercaptoethanol
-
1 mM, 40% inhibition
3-(5-nitrofuran-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
4,7-dicyanobenzofurazan
-
bacteriostatic effect due to inactivation of 2,3-dihydroxyisovalerate dehydratase
benzoquinone
-
-
duroquinone
-
-
hydralazine
-
-
nitric oxide
-
nitric oxide halts bacterial growth via inhibition of the branched-chain amino acid biosynthesis enzyme dihydroxyacid dehydratase
Nitrofurantoin
-
-
NO
-
IlvD is completely inactivated in cells by NO with the concomitant formation of the IlvD-bound dinitrosyl iron complex, DNIC. While the IlvD-bound DNIC and other protein-bound DNICs are stable in cells under anaerobic growth conditions, they are efficiently repaired under aerobic growth conditions even without new protein synthesis, L-cysteine plays an important role, overview
NO
-
inactivation of Rv0189c by NO probably inhibits bacterial growth
p-chloromercuribenzoic acid
-
-
p-hydroxymercuribenzoic acid
-
-
additional information
-
formation of the IlvD-bound DNIC, dinitrosyl-iron complex, and inactivation of the enzyme activity under anaerobic conditions, reaction kinetics of NO and enzyme using diethylamine NONOate as NO donor. GSH fails to prevent the NO-mediated modification of the IlvD [4Fe-4S] cluster regardless of the presence of O2 in the medium, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.97
-
2,3-Dihydroxy-3-methylbutanoate
-
-
2.16
-
2,3-dihydroxy-3-methylpentanoate
-
supernatant enzyme
2.21
-
2,3-dihydroxy-3-methylpentanoate
-
mitochondrial enzyme
3.7
-
2,3-dihydroxy-3-methylpentanoate
-
wild-type enzyme
6.3
-
2,3-dihydroxy-3-methylpentanoate
-
-
8.5
-
2,3-dihydroxy-3-methylpentanoate
-
mutant enzyme 332
0.55
-
2,3-dihydroxybutanoate
-
-
0.54
-
2,3-dihydroxyisovalerate
-
-
0.85
-
2,3-dihydroxyisovalerate
-
mitochondrial enzyme
1.03
-
2,3-dihydroxyisovalerate
-
supernatant enzyme
1.5
-
2,3-dihydroxyisovalerate
-
-
1.5
-
2,3-dihydroxyisovalerate
-
pH 8.0, Tris buffer, since only one of the isomers present in the racemic substrate is active, the corrected Km would be 0.75 mM
2
-
2,3-dihydroxyisovalerate
-
-
2.8
-
2,3-dihydroxyisovalerate
-
-
0.33
-
2R,3R-2,3-dihydroxy-3-methylpentanoate
-
-
0.71
-
2R,3S-2,3-dihydroxy-3-methylpentanoate
-
-
1.78
-
3-cyclopropyl-2,3-dihydroxybutanoate
-
-
1.75
-
D-erythronate
-
-
-
2.42
-
D-gluconate
-
-
3.7
-
DL-2,3-dihydroxyisovalerate
-
pH 8.0, temperature not specified in the publication
0.65
-
L-threonate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.5
-
2,3-Dihydroxy-3-methylbutanoate
-
-
4.6
-
2,3-dihydroxybutanoate
-
-
25
-
2,3-dihydroxyisovalerate
-
-
75.8
-
2,3-dihydroxyisovalerate
-
-
8.3
-
2R,3R-2,3-dihydroxy-3-methylpentanoate
-
-
12.3
-
2R,3S-2,3-dihydroxy-3-methylpentanoate
-
-
5.7
-
3-cyclopropyl-2,3-dihydroxybutanoate
-
-
48.5
-
D-gluconate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.024
-
-
purified native enzyme, pH 8.0, temperature not specified in the publication
0.132
-
-
-
0.416
-
-
-
10.13
-
-
-
additional information
-
-
rapid and sensitive assay
additional information
-
-
-
additional information
-
-
activity stain
additional information
-
-
reverse-phase high-performance liquid chromatography assay
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.7
8
-
2,3-dihydroxy-3-methylpentanoate
7.8
-
-
2,3-dihydroxy-3-methylpentanoate
7.8
-
-
2,3-dihydroxy-3-methylpentanoate; mutant strain 332
7.9
-
-
2,3-dihydroxyisovalerate
7.9
-
-
2,3-dihydroxy-3-methylpentanoate
8
8.2
-
2,3-dihydroxy-3-methylpentanoate, 2,3-dihydroxyisovalerate
8
8.3
-
2,3-dihydroxyisovalerate
8
-
-
assay at
8.2
-
-
2,3-dihydroxyisovalerate
8.2
-
-
2,3-dihydroxy-3-methylpentanoate, wild-type strain
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
pH 7.0: about 40% of maximal activity, pH 9.0: about 25% of maximal activity, 2,3-dihydroxyisovalerate
7.4
9
-
pH 7.4: about 40% of maximal activity, pH 9.0: about 70% of maximal activity, 2,3-dihydroxy-3-methylpentanoate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6.0: about 30% of maximal activity, pH 9.0: about 35% of maximal activity
60
90
-
60C: about 60% of maximal activity, 90C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
upregulation of Rv0189c occurs during the early exponential phase of growth
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12000
-
-
gel filtration
105000
-
-
gel filtration
110000
-
-
native PAGE
125000
-
-
native PAGE
155000
-
-
gel filtration, recombinant thioredoxin-His-tagged IlvD
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 63000, SDS-PAGE
dimer
-
2 * 66000, SDS-PAGE
dimer
-
2 * 66000, SDS-PAGE
homodimer
-
2 * 78300, recombinant thioredoxin-His-tagged IlvD, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
20 min, stable
45
-
-
20 min, about 5% loss of activity
46.5
-
-
20 min, 50% loss of activity, mutant strain 332
50
-
-
20 min, about 25% loss of activity
55
-
-
20 min, about 55% loss of activity
56
-
-
20 min, 50% loss of activity, wild type
60
-
-
20 min, complete loss of activity
70
-
-
2 h, stable
80
-
-
30 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme in crude extract is labile to heat and acid
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
exposure of E. coli cells to 4.2 atm O2 causes complete loss of activity
-
33973
hyperbaric oxygen results in rapid inactivation
-
33971, 33975
inactivation by exposure to hyperbaric O2 is due to the destruction of its catalytically active 4Fe-4S cluster. Reactivation occurs by reconstitution of the enzyme's Fe-S cluster
-
33977
oxidative degradation appears to lead to a complete breakdown of the Fe-S cluster, and the resulting protein cannot by reactivated with Fe2+ and thiol reducing agents
-
33976
5% O2, at 25C, half-life: less than 6 min, under anaerobic conditions the enzyme is stable for more than 8 days
-
33983
when the recombinant enzyme is incubated in 50 mM Tris-HCl buffer at 30C for 2 h under aerobic or anaerobic conditions and the residual activity is measured, no difference is found between aerobic and anaerobic conditions
-
680539
when the recombinant enzyme is incubated in 50 mM Tris-HCl buffer at 30C for 2 h with organic peroxide, the enzyme activity is stable during exposure to 0.5% organic peroxide for 2 h
-
680539
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, about 85% loss of activity after 4 weeks, crude extract is unstable upon storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant thioredoxin-His-tagged IlvD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene ilvD, co-expression with other enzymes of the branched amino acid biosynthesis pathway in Bacillus subtilis strain 168 for production of isobutanol via the Ehrlich pathway, overview. Bacillus subtilis is engineered as the cell factory for isobutanol production due to its high tolerance to isobutanol. Subcloning in Escherichia coli strain JM109
-
gene ilvD, expression in Escherichia coli DH5alpha, overexpression
-
gene ilvD, co-overexpression with genes ilvBCEGHN in Escherichia coli strain W for engineering of L-valine production in fed-batch fermentation, engineering method development and evaluation, overview
-
recombinant expression of IlvD [4Fe-4S] cluster from Escherichia coli
-
gene Rv0189c or ilvD, overexpression of thioredoxin-His-tagged IlvD in Escherichia coli strain OrigamiBL21(DE3). Transcript levels of Rv0189c in sense and antisense transformants of Mycobacterium tuberculosis, phenotype, overview
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
upregulation of Rv0189c occurs during the early exponential phase of growth, under acid stress and ex vivo. Rv0189c expression is upregulated by 1.72fold at pH 4.5 and 1.42fold at pH 5.5, compared to that at pH 7.2, relative gene expression profiles of Rv0189c starved in PBS, overview
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
construction of a valine producer by genetic engineering, mutant strains are resistant against inhibition by branched-chain amino acids L-valine, L-isoleucine and L-leucine, A constructed weak promoter of ilvA or leuA, which is introduced into the Corynebacterium glutamicum chromosome via a gene-replacement technique, reduces the biosynthetic rate of isoleucine or leucine, which lowers the mutant growth rate and increases valine production. Overexpression of ilvD driven by the strong mutant promoter P-ilvDM7 resultsin an even higher level of valine production, engineered strains, overview
additional information
-
engineering of wild-type Corynebacterium glutamicum for growth-decoupled production of 2-ketoisovalerate from glucose by deletion of the aceE gene encoding the E1p subunit of the pyruvate dehydrogenase complex, deletion of the transaminase B gene ilvE, and additional overexpression of the ilvBNCD genes, encoding the L-valine biosynthetic enzymes acetohydroxyacid synthase, acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase. 2-Ketoisovalerate production is further improved by deletion of the pyruvate:quinone oxidoreductase gene pqo. In fed-batch fermentations at high cell densities, the constructed strains produce up to 188 mM 2-ketoisovalerate and show a product yield of about 0.47 mol per mol of glucose and a volumetric productivity of about 4.6 mM 2-ketoisovalerate per h in the overall production phase, overview
additional information
-
construction of a relaxed rel deletion Corynebacterium glutamicum DELTAilvA DELTApanB DELTArel ilvNM13 (pECKAilvBNC) strain with the ilvBNC operon present on the multicopy plasmid pECKA
additional information
-
construction of a relaxed rel deletion Corynebacterium glutamicum DELTAilvA DELTApanB DELTArel ilvNM13 (pECKAilvBNC) strain with the ilvBNC operon present on the multicopy plasmid pECKA
-
additional information
-
construction of strain BL21(DE3) DELTAilvD knockout mutant, functional complementation by Mycobacterium tuberculosis IlvD
additional information
-
enzyme from iv-1 mutant strain 332 differs from the wild type enzyme with respect to heat-inactivation, pH-dependence, and kinetics. The altered structure of the mutant enzyme is the basic defect hindering its incorporation into mitochondria
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
the enzyme is used to quantify and investigate the biological oxidant stress activity of various redox-cycling chemicals. High sensitivity to inactivation by oxidants makes the enzyme useful for identification of compounds which increase oxyradical flux in the cell and for probing their mechanism of action
drug development
-
DHAD can be a potential drug/vaccine target, as it is absent in mammals