Genetic code

NOTE - starting VarNomen version 3 the '*' is used to

indicate a translation stop codon, replacing the 'X' used
previously (see Background).
Nucleotide position in codon
first

second
UCU
UCC
UCA
UCG

C
- Ser
- Ser
- Ser
- Ser

CUU - Leu
CUC - Leu
CUA - Leu
CUG - Leu

CCU
CCC
CCA
CCG

AUU - Ile
AUC - Ile
AUA - Ile
AUG - Met

ACU
ACC
ACA
ACG

GUU - Val
GUC - Val
GUA - Val
GUG - Val

GCU
GCC
GCA
GCG

U
UUU - Phe
UUC - Phe
UUA - Leu
UUG - Leu

third
UAU
UAC
UAA
UAG

A
- Tyr
- Tyr
- *
- *

UGU
UGC
UGA
UGG

G
- Cys
- Cys
- *
- Trp

U
C
A
G

Pro
Pro
Pro
Pro

CAU
CAC
CAA
CAG

His
His
Gln
Gln

CGU
CGC
CGA
CGG

Arg
Arg
Arg
Arg

U
C
A
G

Thr
Thr
Thr
Thr

AAU
AAC
AAA
AAG

Asn
Asn
Lys
Lys

AGU
AGC
AGA
AGG

Ser
Ser
Arg
Arg

U
C
A
G

Ala
Ala
Ala
Ala

GAU
GAC
GAA
GAG

Asp
Asp
Glu
Glu

GGU
GGC
GGA
GGG

Gly
Gly
Gly
Gly

U
C
A
G

Amino acid descriptions

One letter Three letter
Amino acid
code
code
A
Ala
Alanine

Possible codons
GCA, GCC, GCG, GCT

Asx

Asparagine or Aspartic acid AAC, AAT, GAC, GAT

Cys

Cysteine

TGC, TGT

Asp

Aspartic acid

GAC, GAT

Glu

Glutamic acid

GAA, GAG

Phe

Phenylalanine

TTC, TTT

Gly

Glycine

GGA, GGC, GGG, GGT

His

Histidine

CAC, CAT

Ile

Isoleucine

ATA, ATC, ATT

Lys

Lysine

AAA, AAG

Leu

Leucine

CTA, CTC, CTG, CTT, TTA, TTG

Met

Methionine

ATG

Asn

Asparagine

AAC, AAT

Pro

Proline

CCA, CCC, CCG, CCT

Gln

Glutamine

CAA, CAG

Arg

Arginine

AGA, AGG, CGA, CGC, CGG, CGT

Ser

Serine

AGC, AGT, TCA, TCC, TCG, TCT

Thr

Threonine

ACA, ACC, ACG, ACT

Val

Valine

GTA, GTC, GTG, GTT

Trp

Tryptophan

TGG

any codon

NNN

Tyr

Tyrosine

TAC, TAT

Glx

Glutamine or Glutamic acid CAA, CAG, GAA, GAG

stop codon

TAA, TAG, TGA

Amino acid properties

Property

Amino acids

small

Ala, Gly

acidic / amide

Asp, Glu, Asn, Gln

charged

negative

Asp, Glu

positive

Lys, Arg

polar

Ala, Gly, Ser, Thr, Pro

hydrophobic

Val, Leu, Ile, Met

big

Glu, Gln, His, Ile, Lys, Leu,

Met, Phe, Trp, Tyr

small

Ala, Asn, Asp, Cys, Gly, Pro,

Ser, Thr, Val

size

aliphatic

Ile, Leu, Val

aromatic

His, Phe, Tyr, Trp

1. Oxidation and reduction. Enzymes that carry out these reactions are
called oxidoreductases. For example, alcohol dehydrogenase converts primary
alcohols to aldehydes.
In this reaction, ethanol is converted to acetaldehyde, and the cofactor, NAD, is
converted to NADH. In other words, ethanol is oxidized, and NAD is reduced. (The
charges don't balance, because NAD has some other charged groups.) Remember that
in redox reactions, one substrate is oxidized and one is reduced.
2. Group transfer reactions. These enzymes, called transferases, move functional
groups from one molecule to another. For example, alanine aminotransferase shuffles
the alphaamino group between alanine and aspartate:

Other transferases move phosphate groups between ATP and other compounds, sugar residues to
form disaccharides, and so on.
3. Hydrolysis. These enzymes, termed hydrolases, break single bonds by adding the elements
of water. For example, phosphatases break the oxygenphosphorus bond of phosphate esters:
Other hydrolases function as digestive enzymes, for example, by breaking the peptide bonds in
proteins.
4. Formation or removal of a double bond with group transfer. The functional groups
transferred by these lyase enzymes include amino groups, water, and ammonia. For example,
decarboxylases remove CO 2 from alpha or betaketo acids:
Dehydratases remove water, as in fumarase (fumarate hydratase):

Deaminases remove ammonia, for example, in the removal of amino groups from amino acids:
5. Isomerization of functional groups. In many biochemical reactions, the position of a
functional group is changed within a molecule, but the molecule itself contains the same number
and kind of atoms that it did in the beginning. In other words, the substrate and product of the
reaction are isomers. The isomerases (for example, triose phosphate isomerase, shown
following), carry out these rearrangements.
6. Single bond formation by eliminating the elements of water. Hydrolases break bonds by
adding the elements of water; ligases carry out the converse reaction, removing the elements of
water from two functional groups to form a single bond. Synthetases are a subclass of ligases
that use the hydrolysis of ATP to drive this formation. For example, aminoacyltransfer RNA
synthetases join amino acids to their respective transfer RNAs in preparation for protein
synthesis; the action of glycyltRNA synthetase is illustrated in this figure: