TUGAS KEPUSTAKAAN KIMIA

MEMBUAT KUTIPAN DAN BIBLIOGRAFI

UNTUK SUBJEK ASAM AMINO

Oleh :
Arni Al Hikmah Putri
15030194044
Pendidikan Kimia Unggulan 2015

JURUSAN KIMIA
FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM
2017
1. Penemuan Asam Amino
Asam amino yang pertama kali ditemukan adalah aspargin, pada yahun
1806. Yang paling akhir treonin, yang belum teridentifikasi sampai tahun
1938 (Lehninger, 1982 : 108).

2. Klasifikasi Asam Amino

Amino acids are classified as , , , and so on, according to the location
of the amine group on the carbon chain that contains the carboxylic acid
function (Carey, 2008: 1108).

3. Struktur Asam Amino

Nonpolar side chains: Glycine is the smallest amino acid because it has
no side chain. Amino acids with polar but nonionized side chains: Among
amino acids with polar side chains, serine is the smallest; it is not much larger
than alanine. Amino acids with acidic side chains: The electrostatic potential
maps of aspartic acid and glutamic acid are two of the most prominent ones.
Amino acids with basic side chains: Basic amino acids are the opposite of
acidic amino acids. (Carey, 2008 : 1109, 1112)

Amino acids contain both a basic group ( NH2) and an acidic group (
CO2H). In the dry solid state, amino acids exist as dipolar ions, a form in
which the carboxyl group is present as a carboxylate ion, CO2-, and the
amino group is present as an aminium ion, NH3+. (Dipolar ions are also
called zwitterions.) (Solomons, 2014 : 1065)

[ CITATION Sol14 \l 1057 ][ CITATION Cha00 \l 1057 \m Bru14 \m

Bel09 \m Kat11 \m Har12 \m Bel09][ CITATION McM11 \l 1057 ]
[ CITATION Car08 \l 1057 ]

Amino acids with nonpolar, uncharged side chains: e. g., glycine, alanine,
valine, leucine, isoleucine, proline, phenylalanine, tryptophan and
methionine. Amino acids with uncharged, polar side chains: e. g., serine,
threonine, cysteine, tyrosine, asparagine and glutamine. Amino acids with
 charged side chains: e. g., aspartic acid, glutamic acid, histidine, lysine and
arginine. (Belitz, 2009 : 9).

Because amino acids contain both basic amino and acidic carboxyl groups,
they undergo an intramolecular acidbase reaction and exist in aqueous
solution primarily in the form of dipolar ions, called zwitterions (McMurry,
2011 : 504).

The aliphatic side-chain amino acids include glycine, the amino acid in
which R = H, and four amino acids with alkyl side chains. Two amino acid
side chainsserine and threoninecontain alcohol groups. There are two
acidic amino acids (amino acids with two carboxylic acid groups): aspartate
and glutamate. There are two basic amino acids (amino acids with two basic
nitrogen-containing groups): lysine and arginine. Two amino acids
phenylalanine and tyrosinecontain benzene rings (Bruice, 2014 : 1057).

Semua asam amino (20) yang ditemukan pada protein mempunyai ciri
yang sama, gugus karboksil dan gugus amino diikat pada atom karbon yang
sama. Masing-masing berbeda satu dengan yang lain pada rantai sampingnya,
atau gugus R, yang bervariasi dalam struktur, ukuran, muatan listrik, dan
kelarutan dalam air (Lehninger, 1982 : 108).

The general structure of amino acids includes an amino group and a

carboxyl group, both of which are bonded to the a-carbon (the one next to
the carboxyl group). The a-carbon is also bonded to a hydrogen and to the
side chain group, which is represented by the letter R. The R group
determines the identity of the particular amino acid (Campbell & Farrell,
2009 : 65).
An amino acid is a compound that contains at least one amino group (
NH2) and at least one carboxyl group (COOH) (Chang, 2000 : 977).

4. Macam Asam Amino

Our bodies make some of the amino acids shown in the table. The others,
which are called essential amino acids, we have to get from what we eat
(Carey, 2008: 1108).
 Humans are able to synthesize only 11 of the 20 protein amino acids,
called nonessential amino acids. The other 9, called essential amino acids,
are biosynthesized only in plants and microorganisms and must be obtained in
our diet (McMurry, 2011 : 508).

Essential amino acids: Valine, leucine, isoleucine, phenylalanine,

tryptophan, methionine, threonine, histidine (essential for infants), lysine and
arginine (semi-essential). Nonessential amino acids: Glycine, alanine,
proline, serine, cysteine, tyrosine, asparagine, glutamine, aspartic acid and
glutamic acid. (Belitz, 2009 : 9).

Asam amino yang diperlukan untuk sintesis protein dan ini tidak disintesis
sendiri oleh organisme itu tetapi harus terdapat dalam makanannya. Senyawa
ini dirujuk sebagai asam amino esensial (Fessenden & Fessenden, 1986 :
367).

Eight (the essential amino acids) cannot be synthesized in the bodies of

adult humans and must be ingested in food (Hart, dkk, 2012 : 317).

5. Jumlah Asam Amino

Although more than 700 different amino acids are known to occur
naturally, the group of 20 called the standard amino acids listed in Table
27.1 (pages 11101111) commands special attention. These 20 are the amino
acids coded for in DNA-directed protein synthesis. All are -amino acids, and
all but one contain a primary amino function (Carey, 2008: 1108).

In addition to the 20 amino acids commonly found in proteins, 2 others

selenocysteine and pyrrolysineare found in some organisms, and more than
700 nonprotein amino acids are also found in nature (McMurry, 2011 : 505).

The 22 a-amino acids that can be obtained from proteins can be subdivided
into three different groups on the basis of the structures of their side chains,
R. These are given in Table 24.1. Only 20 of the 22 a-amino acids in Table
24.1 are actually used by cells when they synthesize proteins (Solomons,
2014 : 1062)
 There are about 20 amino acids in a protein hydrolysate. With a few
exceptions, their general structure is R CH(NH2) COOH (Belitz, 2009 : 8-
9).

The structures of the 20 most common naturally occurring amino acids

and the frequency with which each occurs in proteins (Bruice, 2014 : 1054).

Among all the possible amino acids, only 20 are usually found in proteins
(Campbell & Farrell, 2009 : 65).

Twenty different amino acids are building blocks of all proteins in the
human body (Chang, 2000 : 978).

6. Sifat Asam Basa Asam Amino

a. Titik Isoelektrik
The isoelectric point (pI ) is the pH at which the concentration of
the dipolar ion is at its maximum and the concentrations of the anions and
cations are equal (Solomons, 2014 : 1065).

The isoelectric point, also called the isoionic point, is the pH at

which the amino acid has no net charge. It is the pH at which the
concentration of the zwitterion is a maximum (Carey, 2008 : 1116).

At some intermediate pH, the amino acid must be exactly balanced

between anionic and cationic forms and exist primarily as the neutral
zwitterion. This pH is called the amino acids isoelectric point, pI
(McMurry, 2011 : 509).

The state of an a-amino acid at any given pH is governed by a

combination of two equilibria, as shown in the above equation for alanine.
The isoelectric point (pI ) of an amino acid such as alanine is the average
of pKa1 and pKa2 (Solomons, 2014 : 1066).

The isoelectric point (pI) of an amino acid is the pH at which it

has no net charge. In other words, it is the pH at which the amount of
positive charge on an amino acid exactly balances the amount of negative
charge (Bruice, 2014 : 1062).
 Titik isoelektrik asam amino pada golongan ini mencerminkan
gugus R mengion yang terkandung (Lehninger, 1982 : 121).

Titik isoelektrik suatu asam amino adalah suatu tetapan fisis.

Nilainya beraneka ragam tetapi berada dalam salah satu dari tiga kisaran
umum (Fessenden & Fessenden, 1982 : 373).

The pH at which a molecule has no net charge is called the

isoelectric pH, or isoelectric point (given the symbol pI). At its
isoelectric pH, a molecule will not migrate in an electric field (Campbell
& Farrell, 2009 : 74).

The intermediate pH at which they do not migrate toward either electrode

is the isoelectric point (Hart, dkk, 2012 : 317).
b. pKa
Glycine is characterized by two pKa values: the one corresponding
to the more acidic site is designated pKa1, the one corresponding to the
less acidic site is designated pKa2 (Carey, 2008 : 1115).

In amino acids the acidity of the carboxyl group is higher and the
basicity of the amino group lower than in the corresponding carboxylic
acids and amines (Belitz, 2009 : 12).

We have seen that compounds exist primarily in their acidic forms

(that is, with their protons attached) in solutions that are more acidic than
their pKa values, and primarily in their basic forms (that is, without their
protons) in solutions that are more basic than their pKa values (Bruice,
2014 : 1060).

Asam amino alanin mempunyai dua daerah berdaya buffer. Salah

satu di antaranya merupakan daerah yang relatif dasar pada kurva,
berpusat kira-kira pada pK 2,34, menunjukkan bahwa alanin adalah
buffer yang baik pada daerah pH sekitar 2,34. Daerah berdaya buffer lain
terletak di antara pH 8,7 dan pH 10,7 (Lehninger, 1982 : 120).

The pKa values of a-carboxyl groups are fairly low, around 2. The
pKa values of amino groups are much higher, with values ranging from 9
to 10.5. The pKa values of side-chain groups, including side-chain
 carboxyl and amino groups, depend on the groups chemical nature
(Campbell & Farrell, 2009 : 73).

7. Stereokimia Asam Amino

The -carbon atom is a chirality center in all the others. Configurations in
amino acids are normally specified by the D, L notational system. All the
chiral amino acids obtained from proteins have the L configuration at their -
carbon atom, meaning that the amine group is at the left when a Fischer
projection is arranged so the carboxyl group is at the top (Carey, 2008 : 1113).

Amino acids, except for glycine, have at least one chiral center and, hence,
are optically active. All amino acids found in proteins have the same
configuration on the -C-atom: they are considered L-amino acids or (S)-
amino acids in the Cahn-Ingold-Prelog system (with L-cysteine an exception;
it is in the (R)-series). D-amino acids (or (R)- amino acids) also occur in
nature (Belitz, 2009 : 13).

Except for glycine, +H3NCH2CO2-, the -carbons of amino acids are

chirality centers. Two enantiomers of each are therefore possible, but nature
uses only one to build proteins (McMurry, 2011 : 508).

The -carbon of all the naturally occurring amino acids (except glycine) is
an asymmetric center. Therefore, 19 of the 20 amino acids can exist as
enantiomers. The D and L notation used for monosaccharides is also used for
amino acids (Bruice, 2014 : 1058).

Semua asam amino baku, kecuali satu mempunyai atom karbon asimetrik,
-karbon. Yang mengikat empat gugus subtituen yang berbeda, yakni, gugus
karboksil, gugus amino, gugus R, dan atom hidrogen (Lehninger, 1982 : 109).

The amino acids found in proteins are not superimposable on their mirror
images (with the exception of glycine). The mirror images known as L-amino
acids are found in proteins; the D-amino acid mirror image molecules are not
(Campbell & Farrell, 2009 : 66).

Except for glycine (aminoacetic acid), protein-derived amino acids are chiral
and have the L configuration (Hart, dkk, 2012 : 317).
8. Kelarutan Asam Amino dalam Air
The solubilities of amino acids in water are highly variable. Besides the
extremely soluble proline, hydroxyproline, glycine and alanine are also quite
soluble. Other amino acids are significantly less soluble, with cystine and
tyrosine having particularly low solubilities (Belitz, 2009 : 14).

Amino Acids are relatively soluble in water but insoluble in hydrocarbons

and are crystalline substances with relatively high melting points (McMurry,
2011 : 504).

Asam amino larut dalam air dan pelarut polar lain, tetapi tidak larut dalam
pelarut nonpolar seperti dietil eter atau benzena (Fessenden & Fessenden,
1986 : 364).

9. Sintesis Asam Amino

One of the oldest methods for the synthesis of amino acids dates back to
the nineteenth century and is simply a nucleophilic substitution in which
ammonia reacts with an -halo carboxylic acid. (Carey, 2008 : 1117)

Treating an aldehyde with ammonia and hydrogen cyanide produces an a-

aminonitrile. Hydrolysis of the nitrile group of the a-aminonitrile converts the
latter to an a-amino acid (Solomons, 2014 : 1069).

Acrylnitrile is catalytically formylated with CO/H2 and the resultant

aldehyde is transformed through a Strecker reaction into glutamic acid
dinitrile which yields D,L-glutamic acid after alkaline hydrolysis (Belitz,
2009 : 32).

One of the oldest methods used to synthesize an amino acid is to employ

an HVZ reaction to replace an a -hydrogen of a carboxylic acid with a
bromine. The resulting a -bromocarboxylic acid can then undergo an SN2
reaction with ammonia to form the amino acid (Bruice, 2014 : 1068).
Sintesis Strecker dari asam amino, yang dikembangkan pada tahun 1850,
merupakan rentetan dua tahap. Tahap pertama ialah reaksi antara suatu
aldehida dan suatu campuran amonia dan HCN untuk menghasilkan suatu
amino nitril. Hidrolisis amino nitril itu menghasilkan asam amino (Fessenden
& Fessenden, 1986 : 369).
10. Reaksi Asam Amino
Amino acids undergo reactions characteristic of both their amine and
carboxylic acid functional groups. Acylation is a typical reaction of the amino
group (Carey, 2008 : 1119).

Amino acids show the usual reactions of both carboxylic acids and amines.
Reaction specificity is due to the presence of both carboxyl and amino groups
and, occasionally, of other functional groups (Belitz, 2009 : 16).

Reaksi ninhidrin digunakan untuk mendeteksi dan menduga asam amino

secara kuantitatif dalam jumlah kecil (Lehninger, 1982 : 125).

Asam-asam amino bereaksi dengan ninhidrin untuk membentuk produk

yang disebut ungu Ruhemann. Reaksi itu biasa digunakan sebagai uji bercak
untuk mendeteksi hadirnya asam amino pada kertas kromatografi (Fessenden
& Fessenden, 1986 : 375).

Amino acids undergo reactions that correspond to each functional group.

In addition to exhibiting both acidic and basic behavior, for example, the
carboxyl group can be esterified and the amino group can be acylated (Hart,
dkk, 2012 : 317).

11. Pemisahan Asam Amino

A mixture of amino acids can be separated by several different techniques,
such as electrophoresis, paper/thin-layer chromatography, and ion-exchange
chromatography (Bruice, 2014 : 1064).
Electrophoresis is a process that makes use of the dependence of charge
on pH to separate amino acids and proteins (Hart, dkk, 2012 : 317).

12. Beberapa reaksi biokimia tentang asam amino

Many of the biochemical reactions of amino acids require pyridoxal 5_-
phosphate (PLP), a component of vitamin B6, as a coenzyme (Carey, 2008 :
1120).

13. Uji Kualitatif dan Kuantitatif Asam Amino

Amino acids may be determined colorimetrically, or by chromatography
techniques or in an amino acid analyzer. For estimating the amino acid
composition of food stuff, feed or any protein, it has to be first hydrolyzed for
 further estimations. The free amino acids may be extracted from the tissues or
foods in ethanol. If the extract sample contains higher amounts of salts and/or
sugars they have to be removed before estimation of amino acids (Katoch,
2011 : 98).

14. Kegunaan Asam Amino

-Aminobutyric acid (GABA), for instance, is found in the brain and acts
as a neurotransmitter; homocysteine is found in blood and is linked to
coronary heart disease; and thyroxine is found in the thyroid gland, where it
acts as a hormone (McMurry, 2011 : 505).
 BIBLIOGRAFI

Belitz, D. H., Grosch, W., & Schieberle, P. (2009). Food Chemistry (Fourth
revised and extended ed.). Heidelberg: Springer.
Bruice, P. Y. (2014). Organic Chemistry (Seventh ed.). USA: Pearson.
Campbell, M. K., & Farrell, S. O. (2009). Biochemistry (Sixth ed.). California:
Thomson Brooks/Cole.
Carey, F. A. (2008). Organic chemistry (Seventh ed.). New York: McGraw Hill.
Chang, R. (2000). Chemistry (Sixth ed.). New York: McGrawGraw Hill.
Fessenden, R. J., & Fessenden, J. S. (1986). Kimia Organik (Third ed., Vol. 2).
(A. H. Pudjaarmaka, Trans.) Jakarta: Penerbit Erlangga.
Hart, D. J., Hadad, C. M., Craine, L. E., & Hart, H. (2012). Organic Chemistry A
Short Course (Thirteenth ed.). California: Brooks/Cole.
Katoch, R. (2011). Analytical Techniques in Biochemistry and Molecular
Biology. New York: Springer.
Lehninger, A. L. (1982). Dasar-Dasar Biokimia (Vol. 1). (M. Thenawijaya,
Trans.) Jakarta: Penerbit Erlangga.
McMurry, J. (2011). Fundamental of Organic Chemistry (Seventh ed.).
California: Brooks/Cole.
Solomons, G., Fryhle, C. B., & Snyder, S. A. (2014). Organic Chemistry
(Eleventh ed.). USA: Wiley.