Enzyme and Coenzyme structures. Vitamins, coenzyme form. Enzyme inhibition

1. Enzyme Structures
and Components
Структура и
составные части
ферментов
Simple Enzymes
Простые ферменты
Complex Enzymes
Сложные ферменты
Holoenzyme
Active form
Холофермент
Активная форма
Protein Residue
Or Apoenzyme
Белковая часть
Или апофермент
Cofactor
non-protein molecules
Кофактор,
Не белковые молекулы
= +
Vitamins
and their derivatives
Витамины
и их производные
Metal ions
and their complexes
Ионы металлов
и их комплексы
Non Vitamins
Невитамины
Coenzymes are not covalently attached to an enzyme, but are very tightly bound. During reaction coenzyme chemically changed
and released. Initial form of coenzymes is regenerated in second, independent reaction. Since coenzymes are chemically changed
as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates,
which are common to many different enzymes.
Кофермент не связан ковалентно с ферментом, но присоединяется во время реакции к молекуле фермента подобно
субстрату, химически изменяется и затем снова освобождается. Первоначальная форма кофермента регенерируется во
второй, независимой реакции.
Prosthetic groups can be covalently bound to enzyme and does not leave enzyme during reaction. The group which have been
bounded to coenzyme is transferred to next substrate or other coenzyme molecule.
Простетические группы прочно связаны с протеиновой молекулой фермента и во время реакции ее не покидает. Группа,
связавшаяся с коферментом, далее переносится на следующий субстрат или другую молекулу кофермента

2. a) Lipoic acid
Ëèï î åâàÿ êèñëî òà
-
OOC (CH2)4 CH
SH
CH2 CH2
SH
HC
S S
CH2
CH2-
OOC (CH2)4
reduced form
âî ññòàí î âëåí í àÿ
ôî ðì à
oxidized form
î êèñëåí í àÿ
ôî ðì à
b) Biotin
Áèî òèí
HN
HC CH
NH
C
H2C CH
S
O
(CH2)4 COO
-
1. Vitamins
Âèòàì èí û
2. Phosphoric acid esters of vitamins
Ñëî æí û å ýô èðû âèòàì èí î â è ô î ñô î ðí î é êèñëî òû
HC
N+
C
C
S
N
NH3C
NH2
CH2
CH2 CH2
CH3
OH
HC
N+
C
C
S
N
NH3C
NH2
CH2
CH2 CH2
CH3
O P
O
-
O
O
P
O-
O
O
-
a) Thiamine pyrophosphate
Òèàì èí ï èðî ô î ñôàò
b) Pyridoxal phosphate
Ï èðèäî êñàëü ô î ñôàò
N
CHO
HO CH2
H3C
O P
O
O-
O
-
N
CH2
HO CH2
H3C
O P
O
O-
O
-
NH2
b) Pyridoxamin phosphate
Ï èðèäî êñàì èí ô î ñôàò
HC
S S
CH2
CH2
C (CH2)4
O
H2N
Lipoamide - Coenzyme form
Ëèï î àì èä - êî ýí çèì í àÿ ô î ðì à
Thiamine pyrophosphate (coenzyme form)
Òèàì èí ï èðî ôî ñô àò (òèàì èí äèô î ñô àò, êî êàðáî êñèëàçà)
- êî ýí çèì í àÿ ô î ðì à
Thiamine - vitamin B1
Òèàì èí - âèòàì èí B1

3. O O
OHHO
HO
OH
H
Ascorbic acid, commonly known as vitamin C
Àñêî ðáèí î âàÿ êèñëî òà, âèòàì èí Ñ
N
N
N
N
OH
H2N
NH
NH
O
COO-
COO-
Folic acid, also known as vitamin B9 or folacin,
as folate, the naturally occurring form.
Ôî ëèåâàÿ êèñëî òà òàêæå èçâåñòí àÿ
êàê âèòàì èí B9 èëè ôî ëàöèí .
Ï ðåäñòàâëåí à â âèäå ï ðèðî äí î é ô î ðì û - ô î ëàòà
N
NCH2
H
H
OH
H
O
H
O
OP
O
N
N
NH2
O
-
O
N+
CH2
H
H
OH
H
OH
H
O
C
O
NH2
OP
-
O
O
P
O
O-
O
-
Nicotinamide adenine dinucleotide phosphate, NADP
+
Í èêî òèí àì èä äèí óêëåî òèä ô î ñô àò èëè Í ÀÄÔ+
N
NCH2
H
H
OH
H
OH
H
O
OP
O
N
N
NH2
O-
O
N+
CH2
H
H
OH
H
OH
H
O
C
O
NH2
OP
-
O
O
Nicotinamide adenine dinucleotide, abbreviated NAD+
Í èêî òèí àì èä àäåí èí äèí óêëåî òèä, Í ÀÄ
+
NADH
Í ÀÄÍ
N
NCH2
H
H
OH
H
OH
H
O
OP
O
N
N
NH2
O-
O
NCH2
H
H
OH
H
OH
H
O
C
O
NH2
OP
-
O
O
HH
H
+
+ 2e
-
N
O
OH
Nicotinic acid, niacine, Vitamin B5 or Vitamin PP
Í èêî òèí î âàÿ êèñëî òà, í èàöèí , âèòàì èí B5 èëè âèòàì èí ÐÐ
N
NH
N
NH3C
H3C O
O
OH
HO
OH
O
P
O
O
-
N
NCH2
H
H
OH
H
OH
H
O
OP
O
N
N
NH2
O
O-
Flavin adenine dinucleotide (FAD)
Ôëàâèí àäåí èí äèí óêëåî òèä (ÔÀÄ)
N
NH
N
NH3C
H3C O
O
OH
HO
OH
OH
Riboflavin, also known as vitamin B2,
Ðèáî ô ëàâèí èëè Âèòàì èí B2

4. cyclo-Adenosine monophosphate (cAMP)
öèêëî -Aäåí î çèí ì î í î ôî ñôàò (öÀÌ Ô)
P
O-
O
N
NCH2
H
H
O
H
OH
H
O
O N
N
NH2
N
NCH2
H
H
OH
H
OH
H
O
OP
O-
N
N
NH2
O
O-
Adenosine monophosphate (AMP)
5'-Adenylic acid
Aäåí î çèí ì î í î ô î ñô àò (ÀÌ Ô)
Adenosine diphosphate (ADP)
Aäåí î çèí äèô î ñô àò (ÀÄÔ)
N
N H2C
H
H
OH
H
OH
H
O
O P
O-
N
N
NH2
O
O P O-
O
O-
N
N H2C
H
H
OH
H
OH
H
O
O P
O-
N
N
NH2
O
O P O
O
O-
P
O
O-
O-
Adenosine triphosphate (ATP)
Aäåí î çèí òðèô î ñô àò (ÀÒÔ)
N
NCH2
H
H
OH
H
OH
H
O
OP
O
-
N
N
OH
O
O
-
NH2
Guanosine monophosphate (GMP)
5'-Guanylic acid
Ãóàí èí ì î í î ôî ñôàò (ÃÌ Ô)
N
NH
N
NH3C
H3C O
O
CH2 (CHOH)3 CH2 O P
O
O-
O-
Flavin mononucleotide (FMN)
Ôëàâèí ì î í î í óêëåî òèä (ÔÌ Í )

5. Ion
Examples of enzymes
containing this ion
Cupric Cytochrome oxidase
Ferrous or Ferric
Catalase
Cytochrome (via Heme)
Nitrogenase
Hydrogenase
Magnesium
Glucose 6-phosphatase
Hexokinase
Manganese Arginase
Molybdenum Nitrate reductase
Nickel Urease
Selenium Glutathione peroxidase
Zinc
Alcohol dehydrogenase
Carbonic anhydrase
DNA polymerase
Ион
Примеры ферментов
содержащих этот ион
Медь Цитохром оксидаза
Железо
Каталаза
Цитохром (посредством Гема)
Нитрогеназа
Гидрогеназа
Магний
Глюкозо-6-фосфатаза
Гексокиназа
Manganese Аргиназа
Молибден Нитрат редуктаза
Никель Уреаза
Селен Глутатион пероксидаза
Цинк
Алкоголь дегидрогеназа
Карбоангидраза
ДНК полимераза
Metal ions
and their complexes
Ионы металлов
и их комплексы

6. How a competitive inhibitor may block
the active site of an enzyme.
Allosteric inhibition and activation of an enzyme.

7. Enzyme inhibition
Class Competitive inhibition · Uncompetitive inhibition · Non-competitive inhibition · Suicide inhibition · Mixed inhibition
Substrate
Oxidoreductase (EC 1) Aromatase · Lipoxygenase · Monoamine oxidase · COX-2 · Xanthine oxidase · Dihydrofolate reductase ·
Ribonucleotide reductase · 5-alpha-reductase
Transferase (EC 2) Integrase · Protein kinase · Reverse transcriptase · COMT · Thymidylate synthase · Dihydropteroate synthetase ·
Farnesyltransferase · GABA transaminase
Hydrolase (EC 3) Acetylcholinesterase · Phosphodiesterase · Protease (ACE, Trypsin) · Histone deacetylase · Dipeptidyl peptidase-4
Lyase (EC 4) Carbonic anhydrase · Dopa decarboxylase
COO
-
CH2
CH2
COO
-
+ FAD
+
COO
-
C
C
COO
-
H
H
succinate dehydrogenase
-
OOC CH2 COO-
X
N
O
O
N
H
O
S
O
HO
CH3
CH3
Penicillin
Transpeptidase
act here

9. A zymogen (or proenzyme) is an inactive enzyme precursor. A zymogen requires a biochemical change (such as a hydrolysis reaction
Revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme. The biochemical
change usually occurs in a lysosome where a specific part of the precursor enzyme is cleaved in order to activate it.
The amino acid chain that is released upon activation is called the activation peptide.