Information on EC 4.2.1.129 - squalene-hopanol cyclase

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

EC NUMBER
COMMENTARY hide
4.2.1.129
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RECOMMENDED NAME
GeneOntology No.
squalene-hopanol cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hopan-22-ol = squalene + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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diploterol and cycloartenol biosynthesis
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hopanoid biosynthesis (bacteria)
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Sesquiterpenoid and triterpenoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
hopan-22-ol hydro-lyase
The enzyme produces the cyclization products hopene (cf. EC 5.4.99.17) and hopanol from squalene at a constant ratio of 5:1.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene shc or hpnF
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-
Manually annotated by BRENDA team
no activity in Escherichia coli
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-
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Manually annotated by BRENDA team
gene shc or hpnF
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hopan-22-ol
squalene + H2O
show the reaction diagram
squalene + H2O
hopan-22-ol
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hopan-22-ol
squalene + H2O
show the reaction diagram
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-
-
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?
squalene + H2O
hopan-22-ol
show the reaction diagram
additional information
?
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P33247
product pattern of alternative substrates, overview
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
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i.e. CHAPS, almost complete inhibition
sodium-taurodeoxycolate
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almost complete inhibition
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.237
squalene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 4.4
squalene
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.07 - 28.2
squalene
496
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 50
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mutant Q262G
45 - 55
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mutant Q262A
50
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mutant P263G, mutant P263A, mutant E45A, mutant R127Q
50 - 60
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mutant Y267A
55
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mutant E93A, mutant W133A
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SHC in vivo is a membrane-associated protein and can be solubilized from cell extracts by nonionic detergents, such as Triton X-100 or octylthioglucopyranoside. The enzyme is attached to the inner side of the cytoplasmic membrane by interactions of hydrophobic residues with the phospholipids. The membrane-binding part of the enzyme is a nonpolar region that is encircled by positive-charged amino acids enforcing the anchoring of the enzyme to the negatively charged surface of the phospholipid membrane
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72300
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x * 72300, about, sequence calculation
76300
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x * 76300, about, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 71600, about, sequence calculation
additional information
each subunit consists of alpha-helical domains that build up a dumbbell-shaped structure. The first domain consists of a regular (alpha/alpha)6 barrel structure, whereas the second domain shows an alpha-barrel structure in a less periodic manner
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and/or recombinant enzyme, SHC in vivo is a membrane-associated protein and can be solubilized from cell extracts by nonionic detergents, such as Triton X-100 or octylthioglucopyranoside
the native enzyme can be solubilized from membranes by Triton X-100 and Tween 80 without loss of activity, but ionic detergents, such as 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), sodium-taurodeoxycolate, and different glucopyranosides, inhibit this enzyme more or less completely
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene shc or hpnF, part of a gene cluster containing four open reading frames, hpnCDEF
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gene shc or hpnF, part of a gene cluster containing six open reading frames, hpnABCDEF
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gene shc, DNA and amino acid sequence determination, expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C435S/D374I/D374V/H451F
site-directed mutagenesis, inactive mutant
D376E
site-directed mutagenesis, inactive mutant
D377C/D377N/Y612A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C
site-directed mutagenesis, inactive mutant
E45A
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production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
E93A
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production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
F365A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F434A
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production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F437A
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production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F601A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F605A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
G262A
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the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
I261A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Q262A
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the mutation results in a greatly enhanced production of hopanol along with the decreased formation of hopene. A high production of hopanol would be explained as follows. The point mutations could give rise to the perturbation around the “front water”. This disordered “front water” cannot correctly act as the catalytic base for the deprotonation reaction to form hopene, and in turn could be placed near to the final hopanyl cation, leading to a high production of hopanol without forming hopene
Q262G/Q262A/P263G/P263A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
R127Q
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production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
T41A
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production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
V380E
site-directed mutagenesis, inactive mutant
V381A/D376C
site-directed mutagenesis, inactive mutant
W133A
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production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
W169F/W169H/W489A/F605K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y267A
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production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
Y420A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y606A/W23V/W495V/W522V/W533A/W591L/W78S/E35Q/E197Q/D530N/T378A
site-directed mutagenesis, the mutant shows the same product pattern and activity as the wild-type
Y609A/Y612A/L607K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview. The phenotype of Y609F mutein is contrarily described in two publications
Y612F/D376E/D376G/D377E/D377G/D377Q/E45A/E45D/F365W/T41A/E93A/R127Q/W133A/Y267A/F434A/F437A/W258L/D350N/D421N/D442N/H451R/D447N/D377N/D313N/E535Q/D374E
site-directed mutagenesis, the mutant shows the same product pattern as the wild-type with less enzyme activity