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CASE REVIEW

Mrs. Pan, 56 Y.O.

CC: Severe pain arround left


upper abdominal

HT/Anamnesis

Physical Examination

CC: since 2 hour ago


Burning pain radiating
to the back
Eat rich fat food
Never experienced this
pain before
A few days before, oily
stools without mucus

Looked unwell
Blood pressure:
Normal
Pulse rate: Normal
Respiratory rate:
Normal
Temperature: Normal
Abdominal tenderness:
+

Diagnose: Pancreas Disorder

Treatment

Pharmachology:

Give enzyme
substitution
Fat soluble vitamin

Non- Pharmachology:

Surgery

Prognosis
Ad vitam

: Ad bonam

Ad Functionam : Dubia Ad bonam

Laboratory Examination

Amylase: 625 IU/L


Lipase: 390 IU/L
SGOT: Normal

CONCEPT MAP
RF :

Mrs Pan 56 Y.O


(identity)

RICH FAT FOOD


FEMALE
OLD

GALL STONE
(etiology)

ENZYME

DEFINITION
CLASSIFICATION
BASIC STRUCTURE
CHARACTERISTIC
MECHANISM
FUNCTION
FACTOR S INFLUENCE
ENZYME ACTIVITY
INHIBITOR AND
ACTIVATOR
KINETIC

BILE DUCT OBSTRUCTION


(Pathogenesys)

PRESS PANCREATIC DUCT


(Pathophysiology)

ENZYME PATHWAY
BLOCKAGE

PANCREAS DISSORDER
(diagnosis)

LEMAK TIDAK TERCERNA

AUTO DIGESTION

NECROSIS PANCREAS CELL


OILY STOOLS

AMYLASE

BURNING PAIN

LIPASE

TREATMENT

BHP PHOP

Pancreas Disorder
1.
2.
3.
4.
5.
6.

Explain the classification and the basic structure of enzyme


Explain the mechanism of action of ezyme
Explain the activator and inhibitor
Explain the function of enzyme
Explain the clinical implication of enzyme assesment
BHP, PHOP, and CRP

ENZYME
Definition
A protein that catalyzes chemical reactions of other substances without itself being destroyed
or altered upon completion of the reactions (Dorlands Dic)
Basic Structure

Substrate: Reactions, substance upon which an enzyme act


Active site: Small part in an enzyme where substrate molecules bind and undergo a chemical
reactions. This active site is very responsoble
HOLOENZYME

PROTEIN

Non Protein
Tight. Stable

Binds transciently

Prostetik
Coenzyme

Cofactor

Holoenzyme: A holoenzyme is complete and catalytically active Apoenzyme + Cofactor =


Holoenzyme
Apoenzyme: inactive protein componenet of holoenzyme separable from nonprotein
component(prosthetic group/coenzyme/cofactor)
Prosthetic Group :
- Very stable, binds with covalent or noncovalent/ionic bonds

Example : Pyidoxal phosphate, Navin mononucleotide, FAD, metal ions Co, Cu, Mg,
Mn, Zn
most common prosthetic group.
Enzyme-metal ion bond : metalloenzyme
Function :
o Facilitate substrate binding and orientation
o To render substrate electrophilic (e -) or neucleophilic (e +) = more

reactive

Cofactor
- Same function as prosthetic group
- Transcient, dissociable bond
- Must be present in enzymes medium
- Commonly metal ion (metal-activated enzymes)

Coenzyme
- Definition: an organic nonprotein molecule, frequently phosphorylated
derivative of water-soluble vitamin
- Function:
o Transport substrates from point of generation to point of utilization
o stabilizes substrate such as hydrogen atoms or hydride ions thath are
unstable in aqueous env. of cell

Characteristic
Enzyme is protein molecule that is a biological catalyst
Increase the rate of a reaction
Enzymes act specifically with only one reactant (called a substrate) to produce products.
Metabolic enzyme reaction are reversible can catalyzed both forward and reverse
reaction.
Enzyme are unaffected by the reactions that they speed up, so they can be reused again
and again.

Enzymes are regulated from a state of low activity to high activity.


Divided by activation:
a. Fischer Lock and Key: The active site has rigid structural features which are
complementary to the substrate

b. Induced Fit: The active site is flexible, possessing a structure complementary to that of
substrate only when the substrate is bound to the enzyme

Divided by reaction
a. Ping-Pong:

Jadi, akan ada substrat (A) yang masuk membentuk product(P) lalu enzyme berubah menjadi
enzyme intermediate(E*), selanjutnya ada substrat baru(B) yang masuk dan membentuk
product baru lainnya(Q) dan enzyme berubah menjadi enzyme semula(E)

b. Bi-bi: Semua substrat direaksikan terlebih dahulu lalu baru dihasilkan products.
Classification
More than 2000 different enzymes are currently known. A system of classification has been
developed that takes into account both their reaction specificity and their substrate specificity. Each
enzyme is entered in the Enzyme Catalogue with a four-digit Enzyme Commission number (EC
number). The first digit indicates membership of one of the six major classes. Enzymes with similar
reaction specificities are grouped in to each of the six major classes:
The oxidoreductases (class 1)
catalyze the transfer of reducing equivalents from one redox system to another.
Ared + Boks
A oks + Bred
Subclass:
- Oxidases: Use oxygen as an electron acceptor but do not incorporate it into
substrate
- Dehydreogenases: use molecules other then oxygen (e.g: NAD+) as an electron
acceptor
- Oxygonases: Directly incorporate oxygen into substrate
- Poroxidases: Use H2O2 as an electrin acceptor
The transferases (class 2) catalyze the transfer of other groups from one molecule to
another.
AB+C
A+BC
Subclasses::
- Methyl transferases: Transfer 1 carbon unit between substrates
- Amino Transferases: Transfer NH2 from amino acids to keto acids
- Kinoses
: Transfer PO3- from ATP to substrate
The hydrolases (class3) are also involved in group transfer, but the acceptor is always a
water molecule.
A B + H2O
A-H + B-OH
Subclasses:
- Phospatases
: Remove PO3- from substrate
- Phosphodiostorases: Cleave phosphodiester bonds
those in nucleid acid
- Proteases
: Cleave amino bonds
proteins
Lyases (class 4, often also referred to as synthases) catalyze reactions involving ei- ther
the cleavage or formation of chemical bonds, with double bonds either arising or
disappearing.
A (XH) B
AX+B-H
Subclasses:
- Decarboxylases : Product CO2 via elimination reactions
- Aldolases
: Product aldehydes via elimination reactions
- Synthases
: Link two molecules without involvement of ATP
The isomerases (class 5) move groups within a molecule, without changing the gross
composition of the substrate.
A
N30 A
Subclasses:
- Racemases : Intercovert L and D Storeoisomers
- Mutases : Transfer groups between atoms within a molecule

The ligation reactions catalyzed by ligases (synthetases, class 6) areenergy-dependent and


are therefore always coupled to the hydrolysis of nucleoside triphosphates.
A + B + ATP A B ADP Pi
Subclasses:
- Carboxylases : use CO2 as substrate
- SYnthetases : link 2 molecules via an ATP dependant reactions
Factors Influence Enzyme Activity
1. pH
Each enzyme functions best within a certain pH range (optimal pH).
When the pH changes, the active site progressively distorts and affects enzyme function.
e.g: - the enzyme pepsin, which works in stomach, functions best in a strongly acidic
environment. - Lipase, an enzyme found in your small intestine, works best in a basic
environment.
2. Temperature
Each enzyme has a temperature optimum, and beyond this point the enzyme's functional
shape is lost. Boiling temperatures will denature most enzymes.
3. Enzyme Concentration
If the amount of enzyme in a reaction is doubled, the amount of substrate converted to
product is doubled.
4. Substrate Consentration
Doubling of the substrate concentration doubles the reaction rates (while the enzyme
concentration is kept constant)
5. Activator
A substance, other than the catalyst or one of the substrates, that increases the rate of a
catalysed reaction without itself being consumed
6. Inhibitor
Enzyme inhibitors are substances which alter the catalytic action of the enzyme and
consequently slow down, or in some cases, stop catalysis.
Activator Substrate that can activate an unactive enzyme, example HCl that activates
pepsinogen to become pepsin.
Inhibitor Substance that inhibits enzyme activity.
1) Irreversible
Although the inhibitor has been taken out from enzyme, the enzyme still cannot work
like previous
2) Reversible
- Competitive: bind in active site of enzyme, so there will be a competition between
inhibitor and substrate to bind with the enzyme
- Non-competitive: bind with side of the enzyme except the active site, that causes
the active side transform, so the enzyme cant bind with the substrate
- Uncompetitive: let the substrate bind with the enzyme first, and it will bind with the
other side of the enzyme. This makes the product isnt like what it is expected.

The Effect Of Enzyme Inhibitor


1. Competitive Inhibition

In the presence of a competitive inhibitor, it takes a higher substrate concentration to achieve the
same velocities that were reached in its absence. So while Vmax can still be reached if sufficient
substrate is available, one-half Vmax requires a higher [S] than before and thus Km is larger.
2. Noncompetitive Inhibition
With noncompetitive inhibition, enzyme molecules that have been bound by the inhibitor are taken
out of the game so
nged because the active site of those enzyme molecules that have
not been inhibited is unchanged.

OILY STOOLS
Digestion of Lipid
Triglycerides at the most abundant lipids in the diet, which consist of a molecule of glycerol bonded
to three fatty acid molecules. Enzymes that split triglycerides and phospholipid are called lipase.
Triglycerides are broken down by pancreatic lipase into fatty acids (short-chain and long-chain fatty
acid) and monoglycerides. The digestions mostly take place in the small intestines. There are three
types of lipase:
1. Lingual lipase/ptyalin
2. Gastric lipase
3. Pancreatic lipase
Before triglycerides can be digested in the intestine, lipid should undergo emulsification first.
Emulsification is a process whereas the large lipid globule is broken down into several small lipid
globules, done by the bile salts which pass through the bile duct from the gall bladder where it is
stored after being produced by the liver.
The amphipathic side of bile salt helps the emulsification process and therefore able to form the
small lipid globules that provide a large surface area allowing pancreatic lipase to function more
effectively.
The long-chain fatty acids and monoglycerides which packed along with fat-soluble vitamins and
cholesterol molecules resulted from the emulsification is called micelles.
When the micelles are about to be absorbed by the villi inside the duodenum, the fatty and the
monoglycerides diffuse out of the micelles into the absorptive cells. Once inside the absorptive cells,
it is covered by a protein and formed chylomicrons. The chylomicrons

Absorption of Lipid in the Small Intestines


Within 10 minutes after absorption, about half of the chylomicrons have already been removed from
the blood as they pass through blood capillaries in the liver and adipose tissue. This removal is
accomplished by an enzyme attached to the apical surface of capillary endothelial cells, called
lipoprotein lipase, that breaks down triglycerides in chylomicrons and other lipoproteins into fatty
acids and glycerol. The fatty acids diffuse into hepatocytes and adipose cells and combine with
glycerol during resynthesize of triglycerides.
Large Intestines Digestion
The final stage of digestion occurs in the colon through the activity of bacteria that inhabit the lumen
and water absorption. Mucus is secreted by the glands of the large intestine, but no enzymes are
secreted. Chyme is prepared for elimination by the action of bacteria, which ferment any remaining
carbohydrates and release hydrogen, carbon dioxide, and methane gases.
Bacteria also decompose bilirubin to simpler pigments, including stercobilin, which gives feces their
brown color. Bacterial products that are absorbed in the colon include several vitamins needed for
normal metabolism, among them some B vitamins and vitamin K.
By the time chyme has remained in the large intestine 310 hours, it has become solid or semisolid
because of water absorption and is now called feces. Chemically, feces consist of water, inorganic
salts, sloughed-off epithelial cells from the mucosa of the gastrointestinal tract, bacteria, and
products of bacterial decomposition, unabsorbed digested materials, and indigestible parts of food.
In this case, the unavailability of pancreas lipase that could enter the intestines resulted in the
undigested fat which comes along the chyme and existed in the final fecal formed oily stools.

Amylase and Lipase increases


Batu empedu memblokir saluran empedu dan saluran pancreas. Rangsangan lemak
yang datang memicu sekresi enzim lipase amylase dan tripsin. Karena adanya akumulasi
enzim-enzim yang tidak tersalurkan ke duodenum menyebabkan lipase mencerna lapisan
lemak (adipose) sehingga terjadi nekrosis kemudian membuka lapisan yang dibawahnya ada
acinar sel yang akan terautodigesti oleh trypsin. Autodigesti tersebut menyebabkan
inflamasi sehingga pembuluh darah membesar dan membuat edema dan membuat
peredaran darah tidak lancar, sehingga terjadi iskemi, yaitu dimana nutrisi dan oksigen tidak
dapat disalurkan ke sel acinar. Hal ini menyebabkan kerusakan sel acinar. Melalui
mekanisme yang masih tidak diketahui, acinar cell injury menyebabkan tripsinogen aktif
sebagai tripsin dan mengautodigesti sel-sel pancreas itu sendiri dan juga terjadi kebocoran
pembuluh darah yang membuat enzim bisa masuk ke pembuluh darah.

PHOP,BHP,CRP
PHOP : Healthy Lifestyle and Family Health Education

Promotive
: Provide education for people about the impact from over-consumption of fat.
Preventive
: Promote the importance of having balanced diet, especially eating foods
containing fat with adequate amount of fat intake (20-35% of total calories) .
Curative
: Promote the importance of eating fibres (in oats) to help lower cholesterol
level.
Rehabilitative : Supervision of a balanced diet, counseling, nutritional rehabilitation.

BHP : Informed Consent


Peraturan Menteri Kesehatan Republik Indonesia nomor 290/Menkes/PER/III/2008 tentang
persetujuan tindakan Kedokteran

Semua tindakan kedokteran yang akan dilakukan terhadap pasien harus mendapat persetujuan,
dapat berupa persetujuan tertulis atau lisan. Untuk yang beresiko tinggi harus tertulis. Apabila
darurat, tidak perlu persetujuan, tetapi harus tertulis di rekam medik dan sesegera mungkin
harus memberikan penjelasan.

Persetujuan bisa dibatalkan, tetapi menjadi tanggung jawab yang membatalkan.

Penjelasan kepada pasien harus dilakukan baik diminta ataupun tidak. Bisa kepada pasien
langsung atau keluarganya apabila pasien tidak sadar.

Penjelasan tentang diagnosis : temuan klinis, diagnosis penyakit, indikasi yangmembutuhkan


dilakukannya tindakan kedokteran, prognosis

Penjelasan tentang tindakan kedokteran: tujuan (preventif, diagnostik, terapeutik,rehabilitatif),


tata cara pelaksanaan, alternatif tindakan lain+ kelebihan dan kekurangan,risiko dan komplikasi,
perluasan tindakan yang mungkin.

Penolakan tindakan kedokteran harus secara tertulis

Deklarasi Lisabon 1991


Pasien berhak untuk menolak pengobatan setelah menerima informasi oleh karena bertolak
belakang pada kepercayaan spiritual. Pasien juga berhak mendapatkan pereda rasa sakit dan harga
diri dan privasi pasien harus dihargai di setiap saatnya.

CRP : Gall stones risk factor


Based on 900 subjects, female sex has a higher risk factor, with the value approaching
9.0. In addition, obesity (BMI > 30), age (> 50years), and a positive family history of gallbladder
disease in a first-degree relative were also found to be significant risk factors.
(Nakeeb, Attila, et al. (2002). Gallstones. Annals of Surgery 235(6): 842849.PMCID: PMC1422514.)

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