15
Dedication
In memory of Gordon Hartman (1936–2004), friend and colleague whose enthusiasm and encyclopaedic knowledge were an asset to all who knew him.
MitochondrionInner membrane
Outer membrane
Intermembranespace
urocanate
histidine
4-imidazolone-5-propionate
2
FIGLU
N 5-formimino -THF
glutamate
NADPH+H+
ATP
ADP+Pi
NADH+H+
g
glutamateg-semialdehyde
(P 5-C)
proline
FADH2
FAD
ornithine
NH4+
N 5,N 10
-methenyl-THF
folatecycle
THF
NAD+
NADP+
NADPH+H+
NADP+
4H+10H+4H+ 4H+ 2H+
4H+ 4H+
H+Pi
H+
QC
NAD+
ADPNADH+H+
ATP
ATP
ComplexComplexComplex
H2O Pi
–O212
2H+
FO
F1
Respiratory chain
ATP
ADP
H2O
a-ketoglutarate glutamate
aspartate
alanine
cysteineserine
glycine
pyruvate
NAD+ NADH+H+
pyruvate
oxaloacetate
lactatemalate
GTPGDP CO2
phosphoenolpyruvate
2-phosphoglycerate
3-phosphoglycerate
NADH+H+
NAD+
H2O
Pi
ATP
ADP
dihydroxyacetonephosphate
ATP ADP
glucose
ATP
ADP
1,3-bisphosphoglycerate
fructose1,6-bisphosphate
fructose6-phosphate
glucose6-phosphate
Pi
Pi
Endoplasmic reticulum
CytosolPi
a-ketoglutarate glutamate
NAD+
NADH+H+
H2O
Complex
4H+
2H+2H+
3H+
6H+
Complex
H+
F1
FADH2
ATPATP
Pi Pi
H+
4H+
H2O –O212
Complex4H+
Q
C
FO
ADP
Pi H+
NADH+H+
malate oxaloacetate
isocitrate
a-ketoglutaratesuccinyl CoAsuccinate
fumarate
a
CoASHH2O
citrate
[cis-aconitate]
CoASH
FAD
acetyl CoA
ADP+Pi
ATP CoASH
HCO3–
GTP GDP
CoASH
CO2
CO2
pyruvate
NAD+
NAD+
NADH+H+
H2O
Pi H+NADH+H+
NAD+
NADH+H+
NAD+
CO2
H2O
H2O
ADP ATPGTP GDP
FADH2
glutamate
NH4+
NADH+H+
FADH2
myristoyl CoA(C14)
C12
C10
C8
C6
C4
(8) acetyl CoA
palmitoylcarnitine
palmitoyl Co A
2 Pi
C14
acetoacetyl CoACoASH
“Ketonebodies"
acetoacetyl CoA
CoASH
hydroxymethylglutaryl CoA(HMGCoA)
acetoacetate
3-hydroxybutyrate
acetyl CoA
CoASH
NADH+H+
FADH2
NADH+H+
FADH2
NADH+H+
FADH2
NADH+H+
FADH2
NADH+H+
FADH2
acetyl CoA
acetyl CoAH2O
NAD+
NADH+H+
CoASH
b-Oxidation
Ketogenesis
glycogen
a (1Æ4) glucoseoligosaccharide(n+1 residues)
a Æ
uridine diphosphateglucose
PPi
UTP
a (1Æ4) glucoseoligosaccharide primer
(n residues)
glycogen(n–1 residues)
glucose1-phosphate
2 Pi
Pi
UDP NADP+ NADPH+H+
6-phosphogluconate6-phosphoglucono-d-lactone
glyceraldehyde3-phosphate
sedoheptulose7-phosphate
erythrose4-phosphate
fructose6-phosphate
fructose6-phosphate
glucose6-phosphate
NADP+ NADPH+H+
glyceraldehyde3-phosphate
fructose6-phosphate
glucose6-phosphate
glyceraldehyde3-phosphate
H2O CO2
Pentose phosphate pathway(hexose monophosphate shunt)
NADP+
NADPH+H+
b b
enoyl ACP
HCO3–+ATP
H++ADP+Pi
CoASH
malonyl ACP
CoASH
C6
malonyl CoA
acetyl CoA
acyl ACP
C4
acetoacetyl ACP
b
acetoacetyl ACP
malonyl CoA
cysteine–SHgroup of
condensingenzyme
hydroxymethylglutaryl CoA(HMGCoA)
acetoacetyl CoA
mevalonate
cholesterolmany intermediates
acetyl CoA
NADP+
NADPH+H+
H2O
D-3-hydroxybutyryl ACP
NADP+
NADPH+H+
H2ONADH+H+ NAD+
NADP+NADPH+H+
citrate
oxaloacetate
ADP+Pi
CoASH
ATP
malate
CO2
acyl carrier protein
CO2
CoASH
b
CO2
O2
tetrahydrobiopterin
dihydrobiopterin
NADP+
NADPH+H+
a-ketoglutarate
glutamate
4-hydroxyphenylpyruvate
homogentisate
4-maleylacetoacetate
fumarylacetoacetate
acetoacetate
phenylalanine
tyrosine
fumarate
oxidised byextrahepatic
tissues
L-DOPA
dopamine
noradrenaline
S-adenosyl-methionine
S-adenosyl-homocysteine
adrenaline
H2O
O2
CO2
O2
H2O
O2
CO2
H2O
Glycolysis
Krebs cycle
Regulatory enzyme
glutamine-PRPPamidotransferase
carbamoylphosphate
synthetase II
palmitoyl CoA (C16)
acyl CoAdehydrogenase
FAD
FADH2
enoyl CoAhydratase
L-3-hydroxyacyl CoAdehydrogenase
L-3-hydroxyacyl CoA
thiolase
3-ketoacyl CoA
CoASH
acetyl CoA
carnitine
(3) palmitateATP
CoASH
PPi+AMP
trans-D2-enoyl CoA
long chain acyl CoA synthetase
H2O
NADH+H+
NAD+
pyrophosphatase
inner CPT
outer CPT
ribulosephosphate
3-epimerase
ribose5-phosphateisomerase
ribulose5-phosphate
xylulose5-phosphate
ribose5-phosphate
transketolase
(thiamine PP)
H2OC16C14C12C10C8
acylcarrierprotein
ATP
ADPglycerol kinase
(not in whiteadipose tissue)
glycerol
tripalmitin(triacylglycerol)
palmitate
esterification
CO2CO2 CO2 CO2 CO2
glycerol3-phosphate
CoASH CoASH CoASH CoASH CoASH
palmitoyl ACP
thio-esterase
3 H2O
lypolysis hormonesensitive lipase(adipose tissue)
Fatty acid synthesis
CoASH
CO2
NAD+
NADH+H+
HCO3–
acetyl CoA
CoASH
CO2
dehydrogenase
CoASH NAD+
CO2
CoASH
argininosuccinate
lyase
synthetase
citrulline
ornithinetranscarbamoylase
2ADP+Pi2ATP
arginine
urea
isovaleryl CoAisobutyryl CoA
methylmalonatesemialdehyde
propionyl CoA
a-methylbutyryl CoA
D-methylmalonyl CoA
L-methylmalonyl CoA
succinylCoA
acetylCoA
acetyl CoA
CoASH
dehydrogenase
glutaryl CoApropionyl CoA
dehydrogenasedehydrogenase
acetyl CoA
THF
Vitamin B12
Odd numberedfatty acids
ornithine
NADH+H+
NAD+
CO2
CO2
CoASH
NADH+H+
NAD+
CO2
NAD+
NADH+H+ NADH+H+
Pi
carbamoylphosphateNH4
+
AMP+PPi
ATPaspartate
fumarate
mutase
acetoacetate
carnitineshuttle
carnitineshuttle
arginase
dehydrogenase
a-ketoisocaproatea-ketoisovalerate
aminotransferaseaminotransferaseaminotransferase
a-keto-b-methylvalerate
isoleucine valine leucine
a-ketobutyrate
threonine
glycine
lysine
saccharopine
2 aminoadipatesemialdehyde
2-aminoadipate
amino-transferase
a-ketoadipate
carnitineshuttle
N5, N10
-methylene THF
Ureacycle
H2O
H2O
CO2
H2O
H2O
CO2
glutamate
IMP
AIR
PRPP
fumarate
aspartate
ADP+Pi
ATP
AMP
ATP
ribose 5-phosphate
b-5-phosphoribosylamine
glycinamideribonucleotide (GAR)
formylglycinamideribonucleotide (FGAR)
FAICAR
AICAR
SAICAR
CAIR
formylglycinamidineribonucleotide (FGAM)
N10-formyl THF
glycine
glutamate
glutamine
glutamine
carbamoyl phosphate
carbamoyl aspartate
dihydroorotate
orotate
OMP(orotidine monophosphate)
aspartate
UMP(uridine monophosphate)
UDP
UTP
FMNH2
2ATP
glutamate
FMN
bicarbonate
GDP
GTP
RNA
ADP
ATP
DNA
dGTP dATP dTTP dCTPUTPCTP
CDP
dCDP
dCMP
dUMP
dTMP
dTDP
UTP
UTP
THF
THF
N 5, N10-methenyl THF
DHF
ATP
ADP+Pi
ATP
ADP+Pi
ATP
ADP+Pi
N10-formylTHF
glutamine
2ADP+Pi
PPi
ADP+Pi
ATP
N 5, N10-methenyl THF
DHF(dihydrofolate)
folate
THF(tetrahydrofolate)
N 5, N10--methylene THF
N10-formyl THF
N5-methyl THF
H2O
NADPH+H+
NADP+
NADPH+H+
NADP+
NADPH+H+
NADP+
NADPH+H+
NADP+
methionine
methyl grouptransferred to
acceptor
SAM(S-adenosylmethionine)
methyltransferase
S-adenosylhomocysteine
homocysteine
cystathionine
homoserine
cysteine
vitamin B6
homocysteinemethyltransferase
N5-methyl THF
THF
homocysteine
vitamin B12
Folatecycle
Methioninesalvagepathway
N-formylkynurenine
kynurenine
3-hydroxykynurenine
3-hydroxyanthranilate
2-amino-3-carboxymuconatesemialdehyde
2-aminomuconatesemialdehyde
2-aminomuconate
tryptophan
alanine
xanthurenate(yellow)
NAD+ andNADP+
synthesis
NH4+
formate
a-ketoadipate
carbamoylphosphatesynthetase I
–CH3
methyl
SAM
Medical Biochemistry at a Glance
Companion website
This book is accompanied by a companion website which contains interactive Multiple-Choice Questions:
www.ataglanceseries.com/medicalbiochemistry
Medical Biochemistry at a GlanceDr J. G. SalwaySchool of Biomedical and Molecular SciencesUniversity of SurreyGuildfordSurrey, UK
Third edition
A John Wiley & Sons, Ltd., Publication
This edition first published 2012 © 2012 by John Wiley & Sons, Ltd.
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First edition published 1996Second edition published 2006Second edition translations:Chinese Translation 2007 Taiwan Yi Hsien Publishing Co. LtdJapanese Translation 2007 Medical Sciences International Ltd, TokyoKorean Translation 2007 E*PUBLIC KOREA Co. LtdPolish Translation 2009 Górnicki Wydawnictwo Medyczne
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Library of Congress Cataloging-in-Publication DataSalway, J. G. Medical biochemistry at a glance. – 3rd ed. / J.G. Salway. p. ; cm. – (At a glance) Includes bibliographical references and index. ISBN-13: 978-0-470-65451-4 (pbk. : alk. paper) ISBN-10: 0-470-65451-1 (pbk. : alk. paper) 1. Biochemistry–Outlines, syllabi, etc. 2. Clinical biochemistry–Outlines, syllabi, etc. I. Title. II. Series: At a glance series (Oxford, England) [DNLM: 1. Biochemical Phenomena. QU 34] QP514.2.G76 2012 612'.015–dc23 2011024248
A catalogue record for this book is available from the British Library.
Set in 9 on 11.5 pt Times by Toppan Best-set Premedia Limited
1 2012
Contents 5
Contents
32 RegulationofglycolysisandKrebscycle 7233 OxidationoffattyacidstoproduceATPinmuscleandketone
bodiesinliver 7434 Regulationoflipolysis,β-oxidation,ketogenesisand
gluconeogenesis 76
Part 6 Lipids and lipid metabolism35 Structureoflipids 7836 PhospholipidsI:phospholipidsandsphingolipids 8037 PhospholipidsII:micelles,liposomes,lipoproteinsand
membranes 8238 Metabolismofcarbohydratetocholesterol 8439 VLDLandLDLmetabolismI:“forward”cholesterol
transport 8640 VLDLandLDLmetabolismII:endogenoustriacylglycerol
transport 8841 HDLmetabolism:“reverse”cholesteroltransport 9042 Absorptionanddisposalofdietarytriacylglycerolsand
cholesterolbychylomicrons 9243 Steroidhormones:aldosterone,cortisol,androgensand
oestrogens 94
Part 7 Metabolism of amino acids and porphyrins44 Ureacycleandoverviewofaminoacidcatabolism 9645 Non-essentialandessentialaminoacids 9846 Aminoacidmetabolism:toenergyasATP;toglucoseand
ketonebodies 10047 Aminoaciddisorders:maplesyrupurinedisease,
homocystinuria,cystinuria,alkaptonuriaandalbinism 10248 Phenylalanineandtyrosinemetabolisminhealthand
disease 10449 Productsoftryptophanandhistidinemetabolism 10650 Haem,bilirubinandporphyria 108
Part 8 Vitamins51 Fat-solublevitaminsI:vitaminsAandD 11052 Fat-solublevitaminsII:vitaminsEandK 11253 Water-solublevitaminsI:thiamin,riboflavin,niacinand
pantothenate 11454 Water-solublevitaminsII:pyridoxalphosphate(B6) 11655 Water-solublevitaminsIII:folateandvitaminB12 11856 Water-solublevitaminsIV:biotinandvitaminC 120
Part 9 Molecular biology57 Thecellcycle 12258 Pyrimidinemetabolism 12459 Purinemetabolism 12660 StructureofDNA 12861 The“centraldogma”ofmolecularbiology 13062 OrganisationofDNAinchromosomes 13263 ReplicationofDNA(part1) 13464 ReplicationofDNA(part2) 13665 DNAdamageandrepair 13866 TranscriptionofDNAtomakemessengerRNA(part1) 14067 TranscriptionofDNAtomakemessengerRNA(part2) 142
Prefacetothethirdedition 7Acknowledgementstothethirdedition 7Figurekey 8SI/massunitconversions 9
Part 1 Acids, bases and pH 1 Acids,basesandhydrogenions(protons) 10 2 UnderstandingpH 12 3 Productionandremovalofprotonsintoandfrom
theblood 14 4 Metabolicalkalosisandmetabolicacidosis 16 5 Respiratoryalkalosisandrespiratoryacidosis 18
Part 2 Structure of amino acids and proteins 6 Aminoacidsandtheprimarystructureofproteins 20 7 Secondarystructureofproteins 22 8 Tertiaryandquaternarystructureandcollagen 24
Part 3 Formation of ATP: oxidation and reduction reactions
9 Oxidation/reductionreactions,coenzymesandprostheticgroups 26
10 AnaerobicproductionofATPbysubstrate-levelphosphorylation,fromphosphocreatineandbytheadenylatekinase(myokinase)reaction 28
11 AerobicproductionofATP 3012 BiosynthesisofATPbyoxidativephosphorylationI 3213 BiosynthesisofATPbyoxidativephosphorylationII 3414 Whathappenswhenprotonsorelectronsleakfromthe
respiratorychain? 3615 Freeradicals,reactiveoxygenspeciesandoxidativedamage 3816 AerobicoxidationofglucosetoprovideenergyasATP 4017 AnaerobicoxidationofglucosebyglycolysistoformATPand
lactate 4218 Anaerobicglycolysisinredbloodcells,2,3-BPG(2,3-DPG)and
theBohreffect 44
Part 4 Carbohydrates19 Carbohydrates 4620 Absorptionofcarbohydratesandmetabolismofgalactose 4821 Fateofglucoseinliver:glycogenesisandlipogenesis 5022 Fructosemetabolism 5223 Glucosehomeostasis 5424 Glucose-stimulatedsecretionofinsulinfromβ-cells 5625 Regulationofglycogenmetabolism 5826 Glycogenbreakdown(glycogenolysis)andglycogenstorage
diseases 6027 Insulinsignaltransductionanddiabetesmellitus 6228 Diabetesmellitus 6429 Alcoholmetabolism:hypoglycaemia,hyperlactataemiaand
steatosis 66
Part 5 Enzymes and regulation of pathways30 Enzymes:nomenclature,kineticsandinhibitors 6831 Regulationofenzymeactivity 70
6 Contents
68 TranscriptionofDNAtomaketransferRNA 14469 TranscriptionofDNAtomakeribosomalRNA 14670 Translationandproteinsynthesis 14871 ComparisonofDNAreplication,DNAtranscriptionandprotein
synthesisineukaryotesandprokaryotes 150
Part 10 Diagnostic clinical biochemistry72 Diagnosticclinicalbiochemistry(withDrJ.W.WrightFRCP,
MRCPath) 152
Index 154
Companion website
ThisbookisaccompaniedbyacompanionwebsitewhichcontainsinteractiveMultiple-ChoiceQuestions:
www.ataglanceseries.com/medicalbiochemistry
Preface to the third edition
The subject matter in Medical Biochemistry at a Glance is selected from the biochemistry content of First Aid for the USMLE Step 1 : the most popular guide used by students preparing for examinations. As such, it is written for medical students, but is equally accessible to students of the biomedical sciences such as biochemists, medical labo-ratory scientists, veterinary scientists, dentists, pharmacologists, phys-iologists, physiotherapists, nutritionists, food scientists, nurses, medical physicists, microbiologists and students of sports science. This book aspires to present medical biochemistry in the concise two - page format of the “ At a Glance ” series.
Students who study biochemistry as a subsidiary part of their course are frequently overwhelmed by the complexity and huge amount of detail involved. Lecturers will be familiar with the anxious expression of students as they complain “ How much of this do we need to know? ” or “ Do we need to memorise all the structural formulae and the chemi-cal reactions? ” In fairness, biochemistry is a complex and heavily detailed subject. Students should have two objectives: (i) to study and understand biochemical concepts and reactions but not necessarily memorise the structural details, (ii) to prepare for examinations by
determining the amount of detail required by intelligent perusal of lecture notes and past examination papers.
Medical Biochemistry at a Glance is written with these two objec-tives in mind. Judicious study of the back inside cover featuring a metabolic chart including formulae and the enzymes catalysing the reactions plus the comprehensive chart on the front inside cover will enable an understanding of metabolic biochemistry. The enzymes which regulate metabolic pathways are indicated in both charts and throughout the book. In the text of the book, complex detail is subju-gated to a faint background so as to emphasise the most important aspects of the topic. However, students must familiarise themselves with the requirements of their particular examination board to deter-mine how much should be trusted to memory.
Finally, the inspiration for Medical Biochemistry at a Glance has developed from my book Metabolism at a Glance . The latter is a more advanced book but the similarity of style between these two books facilitates progression to a higher level by students specialising in metabolism and disorders of metabolism.
Preface and acknowledgements 7
Acknowledgements to the third edition
Following discussion with my editor, it was clear this new, third edition must include a section on “Molecular Biology”: not my strong-est subject. So the start of this book was marked by a four-day trip to Cheshire visiting my friends Dr Peter Barth and his wife Jane. Peter has dedicated his career to molecular biology and so I was most for-tunate when he offered to update me in this fascinating subject. Jane provided excellent food and warm hospitality in their beautiful house. Peter’s patient, clear and authoritative tuition defined the structure of the chapters. We also made time for recreation, and together they gave me a most enjoyable, productive and unforgettable visit. Peter’s support, advice and encouragement continued through to the last moments of the final proofs. This book would not have been possible without Peter’s invaluable help.
Once again I have been very fortunate to work with Elaine Leggett of Oxford Designers & Illustrators and the facilities provided by Mr Richard Corfield and his team. Elaine’s first task was to update the artwork colour scheme from the second edition to full colour. Then, with her customary aplomb and talent she rose to the challenge of interpreting my sketches for the new Molecular Biology section.
At a Christmas drinks party, I met my old colleague Professor Peter Goldfarb. Inspired with Yuletide spirit, he offered help and generously gave his time, wise advice with characteristic attention to detail and constructive criticism.
I am very grateful to readers who have emailed to report errors and to friends and colleagues for expert advice, especially Dr Kimberly Dawdy, Dr Lucy Elphick, Dr Anna Gloyn, Professor Keith Frayn, Mrs
Rosemary James, Professor Gary John, Professor George Kass, Dr Lisa Meira, and Dr Helen Stokes.
Also, I wish again to record my gratitude to those who contributed to the second edition of this book, namely: Professor Loranne Agius, Dr Wynne Aherne, Dr Beatrice Evans, Dr Martyn Egerton, Professor George Elder, Dr Janet Brown, Dr Geoffrey Gibbons, Dr Barry Gould, Dr Bruce Griffin, Professor Stephen Halloran, Professor Chris O’Callaghan, Dr Anna Saada, and Mrs Marie Skerry.
Many reviewers commented on the excellent index compiled by Philip Aslett for the second edition, so I was very pleased when he agreed to help once more.
My editor Martin Davies has been exceptionally supportive. He has replied to my emails with extraordinary promptness and provided every facility requested to ensure efficient completion of the work. Also, it has been a great pleasure to work with other members of a most pro-fessional Wiley-Blackwell team, especially Heather Addison, Lesley Aslett, Helen Harvey, Karen Moore, Laura Murphy, and Beth Norton.
Regrettably, omissions and errors will have occurred and I would be most grateful to have these drawn to my attention.
Finally, I am grateful to my wife Nicky once again for her support, and for tolerating the intrusion of publication deadlines into our social programme; also the accumulation of documents and papers associ-ated with writing this book.
J. G. SalwaySurrey, UK
8 Figure key
Figure key
Disease or poison
Explanation of the cartoon icons
Therapeutic drug
RC C
R R
cyclic AMP
active proteinkinase A
R
inactive protein kinase A
cyclic AMP
–CH3
methyl
SAM
p85P
PDK-1
PAKT
1 2
P
GSK-3
P
αα
P P
active insulin
receptorβ β
-S-S- -S-S--S-S-
IRS-1
P P
PP
Associated with diagnostic blood test
Excretion in urine or faeces. Product may be used in diagnosis
SAM(s-adenosylmethionine) The methyl-donor man
Regulatory enzyme
Fed state or dietary intake
Fasting state, starvation
Pathway operates in cardiac muscle
Pathway operates in skeletal muscle
Pathway operates in liver
Pathway operates in kidney
A hydrophobic group
A hydrophilic group
PKA (protein kinase A) is activated by cyclic AMP which binds to and removes the regulatory (inhibiting) subunits
Insulin receptor is activated by autophosphorylation of the β-subunits when insulin binds to the α-subunits
IRS-1 (insulin receptor substrate-1)
P85. 85 kDa protein is regulatory subunit of PI-3 kinase. Links IRS-1 to PI-3 kinase
AKT (previously known as PKB). A serine/threonine protein kinase. Binds to PIP3
PDK-1. Phosphoinositide- dependent kinase-1 is activated by phosphatidylinositol 3,4,5-trisphosphate
Glycogen synthase kinase -3. Constitutively active in fasting state. Is inhibited when phosphorylated by AKT
Protein phosphatase-1. Activated by insulin-generated signals
PI-3 kinase. Phosphorylates the 3-hydroxyl group of PIP2 to form phosphatidylinositol 3,4,5-trisphosphate
Currently the subject of research, debate or clinical trials
SI/mass unit conversions 9
SI/mass unit conversions
µmol/l mg/dl< 1.2 2.0–2.5 60–120 < 6.0 < 1108–10
mg/dl0.6–1.3mg/dl mg/dl
< 20
160
140
916
15
14
13
12
11
10
9
8
7
6
5
4
3
2
1
0
8
7
6
5
4
3
2
1
0
8
7
6
5
4
3
2
1
0
1
3
4
5
6
7
8
9
10
9
8
7
6
5
4
3
2
1
0
120
100
80
60
40
20
0
0
20.5
1.0
1.5
2.0
2.5
3.0
0
0.5
1.0
1.5
2.0
2.5
3.0
3.5
4.0806.0
5.5
5.0
4.5
4.0
3.5
3.0
2.5
2.0
1.5
1.0
0.5
0
70
60
50
40
30
20
10
0
0
0.5
1.0
1.5
2.0
2.5
3.0
3.5
4.0 800
600
10
15
20
25
30
40
50
60
708090100
130
160
200
550
500
450
400
350
300
250
200
150
100
50
0
350 45
40
35
30
25
20
15
10
5
300
250
200
150
100
50
0
300
250
200
150
100
50
0
2
4
6
8
10
12
14
16
0 0 0
35 8.0
7.9
7.8
7.7
7.6
7.5
7.4
7.3
7.2
7.1
7.0
6.9
6.8
6.7
30
25
20
15
10
5
0
700
600
500
400
300
200
100
0
(¥ 17.1) (¥ 0.25)
Total bilirubin Calcium Creatinine Glucose [H+]
PhosphatePhosphorus
Thyroxine (T4) Triglycerides Urea BUN Total cholesterol
(∏ 17.1) (∏ 0.25)
(¥ 88.4) (¥ 0.056)
(∏ 88.4) (∏ 0.056)mmol/l
mmol/l mmol/l mmol/lρmol/l
µmol/l mmol/l
mg/dl1.9–3.9 7–25 < 1.5
target target3–7 8–200.5–2.0
ng/dl< 133mg/dl mg/dl
0.6–1.25(¥ 0.323) (¥ 12.87)
(∏ 0.323) (∏ 12.87)
(¥ 0.0113) (¥ 0.357)
(∏ 0.0113) (∏ 0.357) mmol/l< 4.0target target
< 155mg/dl
(¥ 0.0259)
(∏ 0.0259)
nmol/l
nmol/lpH = –log10 [H+] in moles
e.g. 100nmol/l
e.g. antilog10 of –7.4 = 0.000000040 mol/l= 40 nmol/l
= –log10 0.000000 = pH 7.0
nmol/lmol/l
(pH 7.35–7.45) (35–45 nmol/l)
