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Information on EC 3.7.1.9 - 2-hydroxymuconate-6-semialdehyde hydrolase

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EC Tree
     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.9 2-hydroxymuconate-6-semialdehyde hydrolase
IUBMB Comments
The enzyme is involved in the degradation of catechols.
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This record set is specific for:
UNIPROT: P96965
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
2-hydroxymuconic semialdehyde hydrolase, meta-cleavage compound hydrolase, hydroxymuconic semialdehyde hydrolase, 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate, 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase, 2-hydroxymuconate semialdehyde hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
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6-isopropyl-HODA hydrolase
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meta-cleavage product hydrolase
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2-hydroxy-6-oxohepta-2,4-dienoate hydrolase
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2-hydroxymuconate semialdehyde hydrolase
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2-hydroxymuconate-semialdehyde hydrolase
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2-hydroxymuconic semialdehyde hydrolase
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HMSH
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-
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HOD hydrolase
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hydrolase, 2-hydroxymuconate semialdehyde
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XylF
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-C bonds in ketonic substances
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-
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxymuconate-6-semialdehyde formylhydrolase
The enzyme is involved in the degradation of catechols.
CAS REGISTRY NUMBER
COMMENTARY hide
54004-61-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
show the reaction diagram
slight hydrolytic activity
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-
?
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate + H2O
?
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0073
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
150 mM phosphate buffer, at pH 7.5 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate
150 mM phosphate buffer, at pH 7.5 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P96965_PSEFL
282
0
31490
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 32000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme A129V, vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A129V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
I199V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
S103A
the mutant has 100000fold lower activity than that of the wild type enzyme
V227I
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
the enzyme activity is stable between pH 7.0 and 9.0
751149
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jun, S.Y.; Fushinobu, S.; Nojiri, H.; Omori, T.; Shoun, H.; Wakagi, T.
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01
Biochim. Biophys. Acta
1764
1159-1166
2006
Pseudomonas fluorescens (P96965), Pseudomonas fluorescens IP01 (P96965), Pseudomonas fluorescens IP01
Manually annotated by BRENDA team
Saku, T.; Fushinobu, S.; Jun, S.; Ikeda, N.; Nojiri, H.; Yamane, H.; Omori, T.; Wakagi, T.
Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IP01
J. Biosci. Bioeng.
93
568-574
2002
Pseudomonas fluorescens (P96965), Pseudomonas fluorescens IP01 (P96965), Pseudomonas fluorescens IP01
Manually annotated by BRENDA team