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Information on EC 4.2.1.157 - (R)-2-hydroxyisocaproyl-CoA dehydratase
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4.2.1.157 (R)-2-hydroxyisocaproyl-CoA dehydrataseIUBMB Comments
The enzyme, isolated from the bacterium Peptoclostridium difficile, is involved in the reductive branch of L-leucine fermentation. It catalyses an alpha/beta-dehydration, which depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI.
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Word Map
- 4.2.1.157
-
mycolic
-
hadab
- tuberculosis
- fas-ii
-
ketyl
- difficile
- clostridia
-
2-hydroxyacyl-coa
- thiacetazone
-
antitubercular
- isoxyl
- nitrogenase
-
3-hydroxyacyl
-
2-hydroxyglutaryl-coa
- benzoyl-coa
-
oxygen-sensitive
- fermentans
-
acidaminococcus
- symbiosum
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
hadbc, (r)-2-hydroxyisocaproyl-coa dehydratase, 2-hydroxyisocaproyl-coa dehydratase, hadbc dehydratase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HadBC dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxy-4-methylpentanoyl-CoA = 4-methylpent-2-enoyl-CoA + H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxy-4-methylpentanoyl-CoA hydro-lyase
The enzyme, isolated from the bacterium Peptoclostridium difficile, is involved in the reductive branch of L-leucine fermentation. It catalyses an alpha/beta-dehydration, which depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
i.e. (R)-2-hydroxyisocaproyl-CoA. The enzyme is involved in the reductive branch of L-leucine fermentation
i.e. isocaprenoyl-CoA
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
the enzyme is involved in fermentation of L-leucine
-
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
i.e. (R)-2-hydroxyisocaproyl-CoA. The enzyme is specific for the R-isomer. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. The activated dehydratase is separated from the activator and ATP. It catalyzes about 10000 dehydration turnovers until the enzyme becomes inactive. Adding activator, ATP, MgCl2, dithionite and dithioerythritol reactivates the enzyme. The enzymatic elimination of H2O probably occurs in syn-fashion. In assays using (E)-isocaprenoyl-CoA as substrate, no activity can be observed suggesting that the dehydration is irreversible under these conditions or the Z-isomer is the correct product
i.e. isocaprenoyl-CoA
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
the catalyzed reaction, an atypical alpha/beta-dehydration, depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein
-
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
-
-
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
Mycobacterium tuberculosis ATCC 25618/ H37Rv
I6WYY7; P9WFJ9
-
-
-
?
additional information
?
-
-
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
additional information
?
-
I6WYY7; P9WFJ9
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25618/ H37Rv
I6WYY7; P9WFJ9
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
i.e. (R)-2-hydroxyisocaproyl-CoA. The enzyme is involved in the reductive branch of L-leucine fermentation
i.e. isocaprenoyl-CoA
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
the enzyme is involved in fermentation of L-leucine
-
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
-
-
-
?
(R)-2-hydroxy-4-methylpentanoyl-CoA
4-methylpent-2-enoyl-CoA + H2O
Mycobacterium tuberculosis ATCC 25618/ H37Rv
I6WYY7; P9WFJ9
-
-
-
?
additional information
?
-
-
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
additional information
?
-
I6WYY7; P9WFJ9
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25618/ H37Rv
I6WYY7; P9WFJ9
1H-NMR analysis of the unsaturations in the mycolic acid of different Mycobacterium tuberculosis wild-type and mutant strains, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
-
a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Iron chelation by bathophenanthroline removes the reduced [4Fe-4S] cluster from the activator protein in an ATP-dependent manner. With ADP, no chelation is observed. Chelation of the oxidised [4Fe-4S] cluster occurs faster with ADP than with ATP
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Zn2+
besides varying amounts of zinc, other metal ions, particularly molybdenum, are not detected in the dehydratase
[4Fe-4S] center
the crystal structure reveals that the heterodimeric protein contains two [4Fe-4S] clusters at a distance of 12 A, each coordinated by three cysteines and one terminal ligand. The cluster in the alpha-subunit is part of the active site. In the absence of substrate, a water/hydroxide ion acts as the fourth ligand. The substrate replaces this ligand and coordinates the cluster via the carbonyl-oxygen of the thioester group. The cluster in the beta-subunit has a terminal sulfhydryl/sulfido ligand and can act as a reservoir to protect the electron from unwanted side reactions via a recycling mechanism
Iron
the enzyme contains 5.7 nonheme iron and 6.1 acid-labile sulfur, determined by chemical analysis
Iron
-
the complex of the heterodimeric dehydratase and the homodimeric activator complex contains per mol 8.5 mol Fe corresponding to the sum of 5.0 mol Fe/mol dehydratase and 3.7 mol Fe/mol activator
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AlF4-
-
AlF4 in combination with ADP traps the interaction of the activator protein with the dehydratase by forming a stable complex containing 1.0 mol homodimeric activator, 1.0 mol heterodimeric dehydratase and 1.2 mol ADP. The formation proceeds much slower than the activation but in an almost irreversible manner. The isolated complex is devoid of any activity
bathophenanthroline
-
a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Iron chelation by bathophenanthroline removes the reduced [4Fe-4S] cluster from the activator protein in an ATP-dependent manner. With ADP, no chelation is observed. Chelation of the oxidised [4Fe-4S] cluster occurs faster with ADP than with ATP
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Reduction of the activator protein and binding of ATP induce conformational changes necessary to transfer the electron to the dehydratase. Interaction of both proteins promotes ATP hydrolysis
-
activator HadI
the activator of the 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile is a homodimeric [4Fe-4S] cluster containing ATPase which is bound in the dimer interface. The crystal structures of the Mg-ADP, Mg-ADPNP, and nucleotide-free states of the reduced activator have been solved at 1.6-3.0 A resolution. Abstraction of the nonacidic beta-proton of the 2-hydroxyacyl-CoA compounds is achieved by the reductive generation of ketyl radicals on the substrate, which is initiated by the transfer of an electron at low redox potentials. The highly energetic electron needed on the dehydratase is donated by a [4Fe-4S] cluster containing ATPase, termed activator. ATP-hydrolysis may not be necessary for electron transfer between the activator and dehydratase. The different propensities of the ATP- versus ADP-bound activator to form a complex with the dehydratase would be in agreement with electron transfer already being enabled by binding of the ATP-bound activator to the dehydratase. ATP-hydrolysis would then be needed to regenerate the ADP-bound state of the activator whose low affinity for the dehydratase would trigger complex dissociation allowing the cycle of reduction of the activator and ATP-induced complex formation between activator and dehydratase to start again
-
activator HadI
the homodimeric activator is extremely oxygen-sensitive. Recombinant HadI activates the dehydratase in the presence of ATP, MgCl2 and a one-electron reducing agent titanium(III) citrate or dithionite
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Revisiting the assignment of Rv0241c to fatty acid synthase type II of Mycobacterium tuberculosis.
Dehydration
Structural Basis for Reductive Radical Formation and Electron Recycling in (R)-2-Hydroxyisocaproyl-CoA Dehydratase.
Tuberculosis
Negative regulation by Ser/Thr phosphorylation of HadAB and HadBC dehydratases from Mycobacterium tuberculosis type II fatty acid synthase system.
Tuberculosis
Physiological Function of Mycobacterial mtFabD, an Essential Malonyl-CoA:AcpM Transacylase of Type 2 Fatty Acid Synthase FASII, in Yeast mct1Delta Cells.
Tuberculosis
Synthesis, antitubercular activity and mechanism of resistance of highly effective thiacetazone analogues.
Tuberculosis
The changes in mycolic acid structures caused by hadC mutation have a dramatic effect on the virulence of Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05 - 0.08
(R)-2-hydroxy-4-methylpentanoyl-CoA
pH 8.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Mycobacterium tuberculosis ATCC 25618/ H37Rv
genes hadB and hadC, or Rv0636 and Rv0637, respectively
I6WYY7; P9WFJ9
UniProt
brenda
hadI, activator of 2-hydroxyisocaproyl-CoA dehydratase
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
I6WYY7; P9WFJ9
Mycobacterium tuberculosis strain H37Ra describes a 1 bp insertion in the MRA0648 gene, the orthologue of the Rv0637 (hadC) gene of Mycobacterium tuberculosis strain H37Rv
evolution
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
Mycobacterium tuberculosis strain H37Ra describes a 1 bp insertion in the MRA0648 gene, the orthologue of the Rv0637 (hadC) gene of Mycobacterium tuberculosis strain H37Rv
-
malfunction
I6WYY7; P9WFJ9
mutation or deletion of hadC affects the biosynthesis of oxygenated mycolic acids, substantially reducing their production level. Myxolic acid distribution is strongly affected by hadC mutation or deletion in Mtb H37Rv with a decrease in the methoxy-mycolic acid content compensated by an increase in alpha-mycolic acids. Additionally, it causes the loss of atypical extra-long mycolic acids. These events have an impact on the morphotype, cording capacity and biofilm growth of the bacilli as well as on their sensitivity to agents such as rifampicin. Deletion of hadC also leads to a dramatic loss of virulence: an almost 4-log drop of the bacterial load in the lungs and spleens of infected immunodeficient mice. Mycolic acids of Mycobacterium tuberculosis and impact of hadC mutation on their relative distribution, Effect of hadC mutation on the morphotype, biofilm growth, tolerance to stresses and virulence of Mycobacterium tuberculosis, phenotypes, detailed overview
malfunction
I6WYY7; P9WFJ9
mutation or deletion of hadC does not affect the growth of Mycobacterium tuberculosis. Myxolic acid distribution is strongly affected by hadC mutation or deletion in Mtb H37Ra with a decrease in the methoxy-mycolic acid content compensated by an increase in alpha-mycolic acids. Complementation of Mycobacterium tuberculosis strain H37Ra with either the wild-type hadC (hadCRv) or both wild-type hadB and hadC allele(s) (hadBCRv) from Mycobacterium tuberculosis strain H37Rv results in similar intermediate phenotypes. Effect of hadC mutation on the morphotype, biofilm growth, tolerance to stresses and virulence of Mycobacterium tuberculosis. Phenotypes, detailed overview
malfunction
Mycobacterium tuberculosis ATCC 25618/ H37Rv
-
mutation or deletion of hadC affects the biosynthesis of oxygenated mycolic acids, substantially reducing their production level. Myxolic acid distribution is strongly affected by hadC mutation or deletion in Mtb H37Rv with a decrease in the methoxy-mycolic acid content compensated by an increase in alpha-mycolic acids. Additionally, it causes the loss of atypical extra-long mycolic acids. These events have an impact on the morphotype, cording capacity and biofilm growth of the bacilli as well as on their sensitivity to agents such as rifampicin. Deletion of hadC also leads to a dramatic loss of virulence: an almost 4-log drop of the bacterial load in the lungs and spleens of infected immunodeficient mice. Mycolic acids of Mycobacterium tuberculosis and impact of hadC mutation on their relative distribution, Effect of hadC mutation on the morphotype, biofilm growth, tolerance to stresses and virulence of Mycobacterium tuberculosis, phenotypes, detailed overview
-
malfunction
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
mutation or deletion of hadC does not affect the growth of Mycobacterium tuberculosis. Myxolic acid distribution is strongly affected by hadC mutation or deletion in Mtb H37Ra with a decrease in the methoxy-mycolic acid content compensated by an increase in alpha-mycolic acids. Complementation of Mycobacterium tuberculosis strain H37Ra with either the wild-type hadC (hadCRv) or both wild-type hadB and hadC allele(s) (hadBCRv) from Mycobacterium tuberculosis strain H37Rv results in similar intermediate phenotypes. Effect of hadC mutation on the morphotype, biofilm growth, tolerance to stresses and virulence of Mycobacterium tuberculosis. Phenotypes, detailed overview
-
metabolism
the enzyme is involved in L-leucine fermentation
metabolism
the enzyme is involved in the reductive branch of L-leucine fermentation
physiological function
I6WYY7; P9WFJ9
involvement of HadBC in the late elongation steps of mycolic acid biosynthesis, involvement of hadC gene in the biosynthesis of atypical extra-long mycolic acids
physiological function
I6WYY7; P9WFJ9
involvement of HadBC in the late elongation steps of mycolic acid biosynthesis, involvement of hadC gene in the biosynthesis of atypical extra-long mycolic acids. Gene hadC is not essential for Mycobacterium tuberculosis growth, inactivity of the hadC gene of H37Ra. Mycolic acids are involved in the pathogenicity of mycobacteria suggesting that there might be a link between the mutation in hadC and the attenuation of Mtb H37Ra
physiological function
Mycobacterium tuberculosis ATCC 25618/ H37Rv
-
involvement of HadBC in the late elongation steps of mycolic acid biosynthesis, involvement of hadC gene in the biosynthesis of atypical extra-long mycolic acids
-
physiological function
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
involvement of HadBC in the late elongation steps of mycolic acid biosynthesis, involvement of hadC gene in the biosynthesis of atypical extra-long mycolic acids. Gene hadC is not essential for Mycobacterium tuberculosis growth, inactivity of the hadC gene of H37Ra. Mycolic acids are involved in the pathogenicity of mycobacteria suggesting that there might be a link between the mutation in hadC and the attenuation of Mtb H37Ra
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A6S6XGC1_9FIRM
376
0
42284
TrEMBL
-
A0A645HTN9_9ZZZZ
199
0
22883
TrEMBL
other Location (Reliability: 2)
A0A644TEX8_9ZZZZ
409
0
46744
TrEMBL
other Location (Reliability: 2)
A0A645GD40_9ZZZZ
227
0
26439
TrEMBL
other Location (Reliability: 3)
A0A645CXB7_9ZZZZ
336
0
38041
TrEMBL
other Location (Reliability: 5)
A0A644Y1C1_9ZZZZ
420
0
47136
TrEMBL
other Location (Reliability: 2)
A0A644XQ29_9ZZZZ
375
0
41983
TrEMBL
other Location (Reliability: 2)
A0A644Y0H0_9ZZZZ
372
0
42032
TrEMBL
other Location (Reliability: 2)
A0A645CTC6_9ZZZZ
388
0
44607
TrEMBL
other Location (Reliability: 3)
A0A645FLZ4_9ZZZZ
144
0
16637
TrEMBL
other Location (Reliability: 2)
A0A645BXT8_9ZZZZ
336
0
37904
TrEMBL
other Location (Reliability: 2)
A0A645K0V0_9ZZZZ
130
0
15001
TrEMBL
other Location (Reliability: 2)
A0A645CLJ1_9ZZZZ
89
0
10395
TrEMBL
other Location (Reliability: 2)
A0A645I7K5_9ZZZZ
192
0
22501
TrEMBL
other Location (Reliability: 4)
A0A645FTW0_9ZZZZ
101
0
11156
TrEMBL
other Location (Reliability: 2)
A0A6S6XLU9_9FIRM
375
0
42391
TrEMBL
-
A0A645GCE5_9ZZZZ
222
0
25233
TrEMBL
other Location (Reliability: 2)
A0A645GTC1_9ZZZZ
170
0
19080
TrEMBL
other Location (Reliability: 1)
A0A645I9I6_9ZZZZ
149
0
17204
TrEMBL
other Location (Reliability: 2)
A0A645H295_9ZZZZ
136
0
15010
TrEMBL
other Location (Reliability: 2)
A0A645EKD3_9ZZZZ
99
0
11218
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
148000
-
1:1 protein complex of the heterodimeric dehydratase (89 kDa) and the homodimeric activator (60 kDa), stable only in the presence of AlF4-, gel filtration
42350
1 * 46578 + 1 * 42350, calculated from sequence
46578
1 * 46578 + 1 * 42350, calculated from sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterodimer
1 * 46578 + 1 * 42350, calculated from sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the dehydratase are grown at 16°C by the vapor diffusion technique from a reservoir solution containing 18-29% (w/v) PEG 3350 and 100 mM BisTris (pH 6.5). The dehydratase is cocrystallized by incubation with 5 mM (R)-2-hydroxyisocaproate 10 min prior to crystallization
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
mutation or deletion of hadC, phenotype, overview. The hadC allele of that Mycobacterium tuberculosis strain H37Ra contains the previously reported single nucleotide insertion (C) in a GC rich region at base pair 88 (Rv0637 numbering), that it causes a frameshift in MRA0648, generating an early stop codon. The deletion mutant is termed H37RaDELTAhadC. No complementation is observed after transformation of Mycobacterium tuberculosis H37RvDELTAhadC mutant with hadC allele from Mycobacterium tuberculosis H37Ra (hadCRa), and the complete deletion of this allele in H37Ra does not significantly affect the mycolic distribution. Complementation of Mycobacterium tuberculosis strain H37Ra with either the wild-type hadC (hadCRv) or both wild-type hadB and hadC allele(s) (hadBCRv) from Mycobacterium tuberculosis strain H37Rv results in similar intermediate phenotypes
additional information
I6WYY7; P9WFJ9
mutation or deletion of hadC, phenotype, overview. The hadC allele of that Mycobacterium tuberculosis strain H37Ra contains the previously reported single nucleotide insertion (C) in a GC rich region at base pair 88 (Rv0637 numbering), that it causes a frameshift in MRA0648, generating an early stop codon. The deletion mutant is termed H37RaDELTAhadC. No complementation is observed after transformation of Mycobacterium tuberculosis H37RvDELTAhadC mutant with hadC allele from Mycobacterium tuberculosis H37Ra (hadCRa), and the complete deletion of this allele in H37Ra does not significantly affect the mycolic distribution. Complementation of Mycobacterium tuberculosis strain H37Ra with either the wild-type hadC (hadCRv) or both wild-type hadB and hadC allele(s) (hadBCRv) from Mycobacterium tuberculosis strain H37Rv results in similar intermediate phenotypes
additional information
Mycobacterium tuberculosis ATCC 25177 / H37Ra
-
mutation or deletion of hadC, phenotype, overview. The hadC allele of that Mycobacterium tuberculosis strain H37Ra contains the previously reported single nucleotide insertion (C) in a GC rich region at base pair 88 (Rv0637 numbering), that it causes a frameshift in MRA0648, generating an early stop codon. The deletion mutant is termed H37RaDELTAhadC. No complementation is observed after transformation of Mycobacterium tuberculosis H37RvDELTAhadC mutant with hadC allele from Mycobacterium tuberculosis H37Ra (hadCRa), and the complete deletion of this allele in H37Ra does not significantly affect the mycolic distribution. Complementation of Mycobacterium tuberculosis strain H37Ra with either the wild-type hadC (hadCRv) or both wild-type hadB and hadC allele(s) (hadBCRv) from Mycobacterium tuberculosis strain H37Rv results in similar intermediate phenotypes
-
additional information
Mycobacterium tuberculosis ATCC 25618/ H37Rv
-
deletion of hadC, phenotype, overview
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes hadB and hadC are encoded in the hadABC locus
I6WYY7; P9WFJ9
the hadBC and hadI genes from Clostridium difficile are functionally expressed in Escherichia coli. They encode the 2-hydroxyisocaproyl-CoA dehydratase HadBC and its activator HadI
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knauer, S.H.; Buckel, W.; Dobbek, H.
On the ATP-dependent activation of the radical enzyme (R)-2-hydroxyisocaproyl-CoA dehydratase
Biochemistry
51
6609-6622
2012
Clostridioides difficile (Q5U925), Clostridioides difficile
brenda
Kim, J.; Darley, D.; Buckel, W.
2-Hydroxyisocaproyl-CoA dehydratase and its activator from Clostridium difficile
FEBS J.
272
550-561
2005
Clostridioides difficile (Q5U923 and Q5U924), Clostridioides difficile
brenda
Knauer, S.H.; Buckel, W.; Dobbek, H.
Structural basis for reductive radical formation and electron recycling in (R)-2-hydroxyisocaproyl-CoA dehydratase
J. Am. Chem. Soc.
133
4342-4347
2011
Clostridioides difficile (Q5U923 and Q5U924), Clostridioides difficile
brenda
Kim, J.; Lu, Y.; Buckel, W.
ATP- and redox-induced conformational changes in the activator of the radical enzyme 2-hydroxyisocaproyl-CoA dehydratase
C. R. Chimie
10
742-747
2007
Clostridioides difficile
-
brenda
Kim, J.; Pierik, A.; Buckel, W.
A complex of 2-hydroxyisocaproyl-Coenzyme A dehydratase and its activator from clostridium difficile stabilized by aluminium tetrafluoride-adenosine diphosphate
Chemphyschem
11
1307-1312
2010
Clostridioides difficile
brenda
Slama, N.; Jamet, S.; Frigui, W.; Pawlik, A.; Bottai, D.; Laval, F.; Constant, P.; Lemassu, A.; Cam, K.; Daffe, M.; Brosch, R.; Eynard, N.; Quemard, A.
The changes in mycolic acid structures caused by hadC mutation have a dramatic effect on the virulence of Mycobacterium tuberculosis
Mol. Microbiol.
99
794-807
2016
Mycobacterium tuberculosis, Mycobacterium tuberculosis (I6WYY7 AND P9WFJ9), Mycobacterium tuberculosis ATCC 25618/ H37Rv (I6WYY7 AND P9WFJ9), Mycobacterium tuberculosis ATCC 25177 / H37Ra
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