Medical Biochemistry: Third Edition
Chapter 2

P. 9: Ka = [H+][A-]/[HA]
Chapter 3

p. 25, Fig. 3.3: D-Fructofuranose

Table 3.2, p.27:
16
16:1; -7, 9
20
CH3(CH2)4CH=CHCH2CH=CHCH2CH=CHCH2CH=CH(CH2)3COOH

Fig. 3.6, p. 28:
Structure PAF:
Structure PA:
Chapter 10

Fig.10.7: Structure B is not explained. Moreover, the second structure (B)
of cholic acid is missing side groups:
1
Chapter 11

Fig.11.6: The structure of thiamin should be as follows:

Fig.11.10: from ascorbic acid to dehydroascorbic acid 2H are released
instead of 2H+. Moreover, the double bond between the carbon-atoms in
dehydroascorbic acid should be a single bond.
Chapter 13


Fig.13.3A: Debranching enzyme should be Branching enzyme.
p. 159, Fig.13.4: (heterotrimeric) G-protein is composed of an ,  and 
subunit instead of , ,  subunits.
Chapter 15

Fig.15.4: Step 1 yields 1.5 ATP rather than 2; for further clarity it may be
nice to keep indicating the position of the  and  carbon-atom (this also
holds for Fig.15.6). Moreover, it may help the students to show the same
amount of carbon-atoms, so that R stands for the same amount of carbonatoms in every round. Step 3 yields 2.5 ATP rather than 3; in Step 4 CoASH enters.
 Table 15.2:
Substrate
Molecular
Net ATP
weight
yield
(mol/mol)
glucose
180
32 (30)
Compare number
with Table 14.1
palmitate
256
106
Compare number
with Fig. 15.3
2
Chapter 16







Learning Objectives: “...and in particular the roles of malonyl-CoA
carboxylase...” should read: acetyl-CoA carboxylase.
Fig.16.2: SH group missing on the left 4’-phosphopantetheine group.
Fig.16.3: In Figure 16.1A, malonyl-CoA is drawn with the S atom, which is
lacking in the structure of malonyl-CoA in Fig.16.3. Moreover, the second
step of the reaction (malonyl transacylase) produces:
p.198: “The synthesis ... and 14 NADPH”.
p.199: Malate + NADP+  pyruvate + CO2 + NADPH + H+
p.199, green box: NADH+ should read NADH.
p.200: Overall reaction: (-CH2-CH2-) + O2 + NADH + H+  (-CH=CH-) +
2H2O + NAD+
Chapter 17



Fig.17.1: Geranyl-PP  Prenylation of proteins. This should be
geranylgeranyl-PP as well as farnesyl.
Fig.17.4: the structures of 2-isopentenyl pyrophosphate and 3,3dimethylallyl pyrophosphate should be, respectively:
Fig.17.6: 7-dehydrocholesterol should be as follows:
3

Fig.17.7: SCAP is missing in this figure, whereas it is described in the text.
Chapter 18


Table 18.1: Diameter (m) should read (nm).
Fig.18.4: cholesterol is displayed as giving direct negative feedback on the
LDL receptor, whereas it is the oxysterols that regulate gene expression.
Chapter 19

Fig.19.9: suggestion: it may increase clarity to explain that only in the
fasting state ketogenic vs glucogenic is relevant.
Chapter 27

Fig.27.4: the structure of PAPS should look like:
Chapter 28


p.381, Fig.28.4: Dehydrolysinonorleucine is missing 2 CH2 groups to the
right of the double bond
p.378, Fig.28.1 Legend: “Three-dimensional structure of collagen.
Collagen monomer strands assume a left-handed, -helical tertiary
structure”  the  should be removed. The same holds for the text on
page 378, right column: “…three -helical peptide chains (see Fig.28.1)”.
4
Chapter 29

Fig.29.3: the structure of heme should be as follows:
Chapter 30

Fig.30.4: adenine should be hypoxanthine:
The structure of IMP is as follows:
5
The structure of GMP is as follows:
The structure of Guanine is as follows:


Fig.30.5: adenine should be adenosine.
p.411, orange box: fluorouridine should be fluorouracil.
Chapter 40

Table 40.2: Goll should be Golf; Gi -subunits do not directly activate PLC,
but may activate PLC indirectly through the regulation of calciumchannels. The -subunits released from Gi are able to directly activate
PLC.
6