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Information on EC 4.2.1.150 - short-chain-enoyl-CoA hydratase and Organism(s) Metallosphaera sedula and UniProt Accession A4YDS4

for references in articles please use BRENDA:EC4.2.1.150
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.150 short-chain-enoyl-CoA hydratase
IUBMB Comments
The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. cf. EC 4.2.1.17, enoyl-CoA hydratase and EC 4.2.1.74, long-chain-enoyl-CoA hydratase.
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This record set is specific for:
Metallosphaera sedula
UNIPROT: A4YDS4
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The taxonomic range for the selected organisms is: Metallosphaera sedula
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
chromodomain y-like protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
crotonyl-CoA hydratase
-
Msed_0399
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
short-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. cf. EC 4.2.1.17, enoyl-CoA hydratase and EC 4.2.1.74, long-chain-enoyl-CoA hydratase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
show the reaction diagram
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
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 0.3
crotonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
crotonyl-CoA
pH 8.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260
crotonyl-CoA
pH 8.0, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
pH 8.0, 65°C, native enzyme, autotrophically- or heterotrophically-grown cell
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
x * 70000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
recombinantly expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hawkins, A.B.; Adams, M.W.; Kelly, R.M.
Conversion of 4-hydroxybutyrate to acetyl coenzyme A and its anapleurosis in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
Appl. Environ. Microbiol.
80
2536-2545
2014
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
Manually annotated by BRENDA team
Ramos-Vera, W.H.; Weiss, M.; Strittmatter, E.; Kockelkorn, D.; Fuchs, G.
Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota
J. Bacteriol.
193
1201-1211
2011
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
Manually annotated by BRENDA team