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