Proline Analogues
Chemical Reviews,
Journal Year:
2024,
Volume and Issue:
124(13), P. 8130 - 8232
Published: June 28, 2024
Within
the
canonical
repertoire
of
amino
acid
involved
in
protein
biogenesis,
proline
plays
a
unique
role
as
an
presenting
modified
backbone
rather
than
side-chain.
Chemical
structures
that
mimic
but
introduce
changes
into
its
specific
molecular
features
are
defined
analogues.
This
review
article
summarizes
existing
chemical,
physicochemical,
and
biochemical
knowledge
about
this
peculiar
family
structures.
We
group
analogues
from
following
compounds:
substituted
prolines,
unsaturated
fused
structures,
ring
size
homologues,
heterocyclic,
e.g.,
pseudoproline,
bridged
proline-resembling
overview
(1)
occurrence
nature
their
chemical
synthesis,
(2)
physicochemical
properties
including
conformation
Language: Английский
Pnictogen‐Bonding Enzymes
Angewandte Chemie International Edition,
Journal Year:
2024,
Volume and Issue:
63(45)
Published: July 5, 2024
Abstract
The
objective
of
this
study
was
to
create
artificial
enzymes
that
capitalize
on
pnictogen
bonding,
a
σ‐hole
interaction
is
essentially
absent
in
biocatalysis.
For
purpose,
stibine
catalysts
were
equipped
with
biotin
derivative
and
combined
streptavidin
mutants
identify
an
efficient
transfer
hydrogenation
catalyst
for
the
reduction
fluorogenic
quinoline
substrate.
Increased
catalytic
activity
from
wild‐type
best
coincides
depth
σ
hole
Sb(V)
center,
emergence
saturation
kinetic
behavior.
Michaelis–Menten
analysis
reveals
transition‐state
recognition
low
micromolar
range,
more
than
three
orders
magnitude
stronger
millimolar
substrate
recognition.
Carboxylates
preferred
by
contribute
hydrogen‐bonded
ion
pairing
anion‐π
interactions
emerging
pyridinium
product.
challenging
stereoselectivity
aqueous
systems
further
emphasizes
compatibility
bonding
higher
order
catalysis.
Language: Английский
Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis
Chemical Reviews,
Journal Year:
2024,
Volume and Issue:
124(19), P. 10877 - 10923
Published: Sept. 27, 2024
Biocatalysis
has
become
an
important
component
of
modern
organic
chemistry,
presenting
efficient
and
environmentally
friendly
approach
to
synthetic
transformations.
Advances
in
molecular
biology,
computational
modeling,
protein
engineering
have
unlocked
the
full
potential
enzymes
various
industrial
applications.
However,
inherent
limitations
natural
building
blocks
sparked
a
revolutionary
shift.
Language: Английский
Enzymatic Synthesis of Saturated Bioisosteres of Ortho‐Substituted Benzenes by Artificial Photoenzyme
Chemistry - A European Journal,
Journal Year:
2025,
Volume and Issue:
unknown
Published: Feb. 17, 2025
Saturated
bioisosteres
of
ortho-substituted
benzenes
are
significant
interest
due
to
their
enhanced
pharmacokinetic
properties,
such
as
improved
metabolic
stability
and
reduced
toxicity,
making
them
valuable
in
drug
design
development.
However,
efficient
synthesis
remains
a
challenge
organic
chemistry.
Herein,
we
report
the
biocatalytic
saturated
using
engineered
artificial
photoenzymes.
The
photoenzyme,
incorporating
genetically
encoded
unnatural
amino
acids
with
benzophenone
photosensitizer
residue,
facilitate
formation
chiral
moderate
enantiomeric
excess
via
energy
transfer
process.
Our
results
demonstrate
versatility
photoenzymes
mediating
new-to-nature
reactions
that
difficult
achieve
conventional
chemical
or
enzymatic
methods.
Language: Английский
Design and Evolution of an Artificial Friedel–Crafts Alkylation Enzyme Featuring an Organoboronic Acid Residue
Shu‐Bin Mou,
No information about this author
Kai‐Yue Chen,
No information about this author
Thittaya Kunthic
No information about this author
et al.
Journal of the American Chemical Society,
Journal Year:
2024,
Volume and Issue:
146(39), P. 26676 - 26686
Published: Aug. 27, 2024
Creating
artificial
enzymes
by
the
genetic
incorporation
of
noncanonical
amino
acids
with
catalytic
side
chains
would
expand
enzyme
chemistries
that
have
not
been
discovered
in
nature.
Here,
we
report
design
an
uses
Language: Английский
Pnictogen‐Bonding Enzymes
Angewandte Chemie,
Journal Year:
2024,
Volume and Issue:
136(45)
Published: July 5, 2024
Abstract
The
objective
of
this
study
was
to
create
artificial
enzymes
that
capitalize
on
pnictogen
bonding,
a
σ‐hole
interaction
is
essentially
absent
in
biocatalysis.
For
purpose,
stibine
catalysts
were
equipped
with
biotin
derivative
and
combined
streptavidin
mutants
identify
an
efficient
transfer
hydrogenation
catalyst
for
the
reduction
fluorogenic
quinoline
substrate.
Increased
catalytic
activity
from
wild‐type
best
coincides
depth
σ
hole
Sb(V)
center,
emergence
saturation
kinetic
behavior.
Michaelis–Menten
analysis
reveals
transition‐state
recognition
low
micromolar
range,
more
than
three
orders
magnitude
stronger
millimolar
substrate
recognition.
Carboxylates
preferred
by
contribute
hydrogen‐bonded
ion
pairing
anion‐π
interactions
emerging
pyridinium
product.
challenging
stereoselectivity
aqueous
systems
further
emphasizes
compatibility
bonding
higher
order
catalysis.
Language: Английский