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FMGE decks > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

farbar’s ds., which enzyme deficient?

A

ceramidase enzyme

c/f– small joint pain

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2
Q

Tangier’s ds., which metabolism is defective?

A

orange colored tonsils– pathognomic

cholesterol metabolism defective

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3
Q

Km high in which of them, Hexo or Glucokinase?

A

Glucokinase

low in hexokinase

(Km direcetly proportional to 1/ affinity)

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4
Q

hexokinase and glucokinase belongs to which group of enzymes?

A

Transferase

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5
Q

all enzymes are proteins except?

A

Ribozymes (RNA with enzyme activity)

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6
Q

LDH 1,2 AND 5 LOCATIONS?

A

LDH1- HEART
LDH2- RBC
LDH5- LIVER

BLOOD- LDH2> LDH1

MI- LDH1> LDH2

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7
Q

FLIPPED PATTERN OF LDH SEEN IN?

A

Myocardial infarction

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8
Q

tryptophan has which type of ring in its structure?

A

Indol ring

Tryptophan—Serotonin (5 HIAA)—- Melatonin (HIAA)

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9
Q

just remember this..

A

60 mg of tryptophan give rise to 1mg of niacin (vit B3)

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10
Q

Tryptophan to niacin needs which vitamin?

A

Vit B6

B6 def.– increase xanthurenic acid and decrease niacin

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11
Q

pellagra seen in which vit def.?

A

Niacin (b3) def.

maize diet (staple diet)

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12
Q

just remember—

A

carcinoid syndrome

24 hour urinary HIAA increased

most of tryptophan——-serotonin —- increase HIAA
but Niacin will be decreased.—- pellagra symptoms

c/f– endocardial fibrosis

flushing

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13
Q

hartnup ds., which defect?

A

AR

absorption of tryptophan and neural AA in intestine and renal tubule is defective

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14
Q

just remember…

A

tryptophan absorb maximum light at 260-280 nm

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15
Q

what is atkin’s diet?

A

Low calorie and low carb diet

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16
Q

just remember..

A

insulin removes phosphate from enzymes and decrease cAMP

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17
Q

OH has tendency to attach with?

A

phosphate

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18
Q

3 AA with OH group?

A

Tyrosine
Threonine
Serine

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19
Q

just remember…-

A

all monosaccharides are reducing sugar as they have free functional group

Imp- Reducing sugar gives Benedict’s test positive in urine sample

Normal color- Blue

Highest sugar content gives brick red color

color changes- viBGYOR

pyq- Benedict’s test is semiquantitative test.

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20
Q

what are enantiomers?

A

mirror images of each other

e.g., D and L glucose

OH orientation at panultimate carbon (5th carbon)

Note- all carbs in our body are found in D forms only

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21
Q

what is epimerism?

A

OH orientation at other than panultimate carbon.

IMP— e.g., – Glucose and Mannose at C2

Glucose and Galactose at C4

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22
Q

what is Anomerism?

A
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23
Q

dietary fibers reduce which thing?

A

total cholesterol and LDL

dec. post prandial blood glucose

make bulk of feces

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24
Q

Mucopolysaccharides (GAGs) made up of?

A

acidic sugar (negative charge) + amino sugar (positive charge)

e.g.- Hyaluronic acid (no sulphate)— imp.— found in synovial fluid and vitreous humour—–responsible for wound healing

Keratan sulphate– responsible for transparency of cornea

– Has no acid (COOH)
– Has no uronic acid

Heparin
Heparan sulphate
chondroitin sulphate
dermatan sulphate

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25
Q

Mucopolysaccharidosis (MPS) c/f?

A

these are lysosomal storage ds.—- all are AR except hunter’s ds.— XR

MPS 1 H- HURLER DS.— COMPLETE IDURONIDASE ENZYME DEF.– Mental retrdation present

MPS 1 S- Scheie ds.– partial iduronidase def.— no mental retardation

MPS 2- Hunter ds.– Iduronate sulfatase def.

  • no corneal clouding– no vision issue

MPS 3- SANFILLIPO—Most common

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26
Q

3 IRREVERSIBLE ENZYMES OF GLYCOLYSIS?

A
  1. hexokinase
  2. PFK— rate limiting enzyme
  3. Pyruvate kinase
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27
Q

just rememer…

A

all kinases are transferase

all kinase require Mg2+ as cofactor

if kinase is involved in any reaction, ATP is used or produced.

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28
Q

In aerobic glycolysis, net gain of ATP?

A

7

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29
Q

IN ANAEROBIC GLYCOLYSIS, NET ATP GAIN?

A

2 ATP only

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30
Q

ATP produced by them:

NADH, FADH,NADPH

A

NADH- 2.5 ATP
FADH- 1.5 ATP
NADPH- 0 ATP

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31
Q

JUST REMEMBER..

A

IF KINASE PRODUCES ATP, THIS IS K/A SUBSTRATE LEVEL PHOSPHORYLATION.

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32
Q

Enolase enzyme is inhibited by?

A

NaF— used for blood glucose estimation

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33
Q

most common enzyme def. leading to hemolytic anemia?

A

G6PD def., lactate high

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34
Q

2nd most common enzyme def., leading to hemolytic anemia?

A

Pyruvate kinase def., Lactate is low

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35
Q

exercise intolerance and low lactate levels, diagnosis?

A

PFK enzyme def.— Type 7 glycogen storage ds.

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36
Q

1 acetyl coA prodcues how many ATPs through kreb’s cycle?

A

10 ATP

so, 2 produces 20 atp

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37
Q

Cofactor for oxidative decarboxylation?

A

B1

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38
Q

cofactor for NADH?

A

B3

39
Q

FADH cofactor?

A

B2

40
Q

CoA, cofactor?

A

B5

41
Q

ETC complex 1 name?

A

NADH CO Q Reductase

42
Q

inhibitor of complex 1?

A

RotenONE

Piercidin

43
Q

just remember?

A

if removing H== oxidation

if adding H– Reduction

44
Q

inhibitor of complex 3?

A

BAL (British Antilewisite)
used in As/Ag poisoning

Antimycin (chemical used in fishery)

Phenformin (not used nowadays— cause lactic acidosis)

Metformin

45
Q

inhibitor of complex 4?

A

CN (cyanide)

CO (carbon mono oxide )

H2S

Azide

46
Q

inhibitor of complex 2?

A

Malonate

Carboxin

TTFA

47
Q

inhibitor of complex 5?

A

Oligomycin==== inhibit F0 (ADP TO ATP conversion)

48
Q

uncouplers of ETC?

A

any compound which cause H+ ion leakage via Inner mitochondrial membrane.

Natural Uncouplers:

Thermogenin=== have F1 but no F0

Thyroxine
Long chain FA
Unconj. bilirubin

other:
2,4 Dinitrophenol (DNP)
Dinitrocresol

49
Q

rate limiting enzyme of HMP shunt?

A

G6PDehydrogenase

50
Q

HMP SHUNT occur in?

A

Cytosol

51
Q

to detect B2 def., we measure which enzyme activity in rbc?

A

Glutathion reductase

52
Q

Von gierke’s ds., which enzyme def.?

A

Glucose 6 Phosphatase def.

C/f- muscles are not affected as they lack this enzyme already

fasting hypoglycemia (severe)

hepatomegaly

no gluconeogenesis

Kidneys are enlarged

53
Q

Pompe’s ds., which enzyme def.? Type 2 GSD

A

acid maltase def.

C/f- hypertrophic cardiomyopathy

54
Q

Cori’s/ Forbe’s/Limit dextrinosis ds., which enzyme def.? Type 3 GSD?

A

DEBRANCHING Enzyme def.

C/f—- abnormal glycogen stored

fasting hypoglycemia

hepatomegaly

myopathy

cures itself—– by the puberty age

55
Q

Type 4 GSD– Anderson ds., which enzyme def.?

A

Branching enzyme def.

C/f- amylopectin like abnormal glycogen accumulate

death occur by 4 yrs

56
Q

Type 5 GSD== Mc Ardle’s ds.?

A

Muscle phosphorylase def.

C/f— exercise intolerance- Rhabdomyolysis– burgendy color urine

low lactic acidosis

57
Q

Type 6 GSD, Her’s ds?

A

Liver phosphorylase def.

c/f— mild symptoms

58
Q

activator of glycogen phosphorylation in muscle?

A

Calcium

59
Q

Gluconeogenesis occur in?

A

Cytoplasm and Mitochondria

60
Q

not substrate for gluconeogenesis?

A

pure ketogenic amino acid=== Leucine, Lysine

61
Q

Glucose 6 phosphatase present in?

A

SER (smooth endo reticulum)

62
Q

MC FA synthesis?

A

palmitic acid

63
Q

Rothras test is used for?

A

Ketone bodies detection

gives purple color

64
Q

Thiophorase is absent in which organ?

A

Liver

can synthesis ketone bodies but can not utilize ketone body due to this enzyme def.

65
Q

alpha oxidation takes place in?

A

Endo reticulum and peroxisome

66
Q

REFSUM DISEASE?

A

peroximal disorder (impaired alpha oxidation of branched chain FA)

e.g, Phytanoyl coA

symptoms- retinitis pigmentosa, Icthyosis, Peripheral neuropathy

67
Q

omega oxidation occurs in?

A

SER

68
Q

ZELL WEGER SYNDROME (cerebro hepato renal)?

A

defect in peroximal function

VLCFA oxidation is altered (it accumulates)—PYQ,

alpha oxidation also affected (branched chain FA)

symptoms- seizures, mongloid face

69
Q

beta oxidation of odd chain FA

A

PROPIONIC ACID (PROPIONYL coA)

70
Q

How HDL works?

A

by making bad cholesterol into cholesterol ester (reverse cholesterol transport) with help of LCAT enzyme (lecithin cholesterol acyl transferase)

Apo A1 is activator of this enzyme.

DEF.- if partial– Fish eye ds. (corneal opacity)

NO RUM disease– ESRD+ Corneal opacity

71
Q

All sphingolipoitosis (LSD)…

A

all have MR– except Gaucher’s ds.

all are AR– except Fabry’s ds.

All have cherry red spot except Gaucher and Fabry’s ds’

72
Q

basic AA are?

A

more basic—Arginine> Lysine> Histidine

73
Q

In electrophoresis, movement depends on?

A

charge, size, shape —- all of them

74
Q

Acidic AA are?

A

aspartic acid, glutamic acid

75
Q

Amino acid which are polar with ccharge?

A

Basic AA
His
ARG
LY

ACIDIC AA

ASP
GL

76
Q

aromatic aa ?

A

phenylalalnine, tyrosine,

77
Q

Phenylketonuria, which enzyme def.?

A

Phenylalanine hydroxylase

78
Q

Formation of GLUTAMATE?

A

Alanine give NH3 group to alpha- ketoglutarate to form Glutamate.

79
Q

Which 3 AA does not show transamination?

A

Po Ly Thene

Proline
Lysine
Threonine

other 17 AA shows transamination

80
Q

In Urea cycle defect/ hyperammonimea, which intermediate of kreb cycle will be depleted?

A

Alpha- ketoglutarate

81
Q

connecting link between kreb cycle and urea cycle?

A

Fumarate

82
Q

connecting AA between Kreb cycle and Urea cycle?

A

Aspartate

83
Q

difference between Hyperammonemia Type 1 and 2?

A

in Type 2 (OTC def.)– Oroticaciduria

in Type 1 (CPS 1)– normal orotic acid

84
Q

Urea C AND N atoms origins?

A

C= CO2
N= NH3
N= Aspartate

85
Q

Helicase funciton?

A

seperate ds DNA

use ATP

produce supercoiling

86
Q

Topoisomerase function?

A

Topo 1– cut one strand

Topo 2– cut both strands

remove supercoiling

NOTE=== In prokaryotes, DNA gyrase in place of topo…

87
Q

Primase fucntion?

A

synthesise primer

one primer for leading strand (synthesis occur continuously)

multi primer for lagging stand (synthesis in fragments)

88
Q

DNA POLYMERASE 3 function?

A

complete leading strand (form DNA)

small fragment on lagging strand— c/a OKAZAKI fragment

89
Q

DNA POLYMERASE 1 function?

A

remove primer in 5’ to 3’ direction from both leading and lagging strands

AND FILL THE GAP ON LAGGING STRAND

small portion of DNA is lost after each replication——TELOMER (TTAGGG)

90
Q

DNA LIGASE FUNCTION?

A

act only on lagging strand and join the fragments

91
Q

what is Heyflick limit?

A

depending on telomer, cell can divide upto 40-60 times

92
Q
A
92
Q

post transcriptional modification of mRNA?

A
  1. CAPPING– occur at 5’ end– it helps to initiate translation (protein synthesis)
  2. poly A tail attachment at 3’ end AAUAAA (signal sequence) ==== stabilize RNA and help in exit from Nucleus
  3. SPLICING— removal of intron— DONE BY SnRNA
93
Q
A

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