encounter carbohydrates groups which are covalently attached to structural features,
which have no catalytic activity but they support E
z
m in stability and solubility
(Edsall and Wyman 1958). Other factors which are associated in E
z
m activity are
cofactors metal ions and low molecular weight organic molecules i.e. co E
z
m . These
may be loosely or tightly bound by monovalent or covalent forces, contributing to
both E
z
m activity and stability (Morr and Ha 1993). E
z
m are named by adding the
suffix “-ase” to substrate e.g.; DNA polymerase E
z
m catalyzes polymerization of
nucleotides to form DNA (Gonzalez-Perez and Vereijken 2007). Urease E
z
m catalyzes urea hydrolysis, etc. Based on functions some E
z
m are also named e.g. pepsin
a digestive E
z
m , derived from Greek word Pepsis’ means digestion; lysozyme
responsible for cell wall lysis of bacteria (Ordonez et al. 2001). It derives some E
z
m
names from their source from where they are obtained, e.g. trypsin is produced by
pancreatic tissue after rubbing it with glycerin hence is named after Greek word
“tryein” meaning “to wear down”. As the time passes away, several new E
z
m are
discovered, some E
z
m have multiple names. To overcome these problems, they are
classified E
z
m based on the R e
at they catalyze after the international agreement
(Chandi and Sogi 2007). So, it classifies E
z
m according to the report of a
Nomenclature committee appointed by the International Union of Biochemistry. As
a result, all E
z
m get a formal E.C. (E
z
m Commission) number and some have their
trivial names (Hamada 2000). The E
z
m commission (EC) numbers divide E
z
m in
order to six major groups according to the R e
at catalyzed (Table 23.9).
23.6.2 Chemical Nature and Properties of E
z m
As discussed above, all E
z
m are p
R
t , and even it is found that it also acts on some
RNA molecules. Each E
z
m has its own specific structure and specific conformation,
which are essential things for catalytic activity (Garfin 2003). Holo E
z
m which
comprises of Apo E
z
m (the p
R
t part) and a co E
z
m (non- p
R
t organic part) is the
functional unit of the E
z
m . The non-p
R
t moiety, which is covalently bound with the
Apo E
z
m termed as prosthetic group, is the integral part of E
z
m structure. Dialysis
can separate the co E
z
m from the E
z
m , whereas they cannot separate the prosthetic
group (Aguilar 2004). If E
z
m is made up of a single poly P E
pt , it is referred as
monomeric E
z
m , if over one poly P E
pt chain present, known as oligomeric E
z
m , e.g.
lactate dehydrogenase. Multi E
z
m complexes possessing E
z
m have specific sites to
catalyze uncommon R e
at in a sequence. Some process can regulate E
z
m activity such
as phosphorylation, glycosylation. These processes alter the structure of a p
R
t found
in the E
z
m . It requires E
z
m in very minute quantity (Aguilar and Hearn 1996). It
does not absorb them in the overall E
z
m R e
at
, rather is received whole after completion of R e
at
. E
z
m do not alter the equilibrium constant (K) of a R e
at but only
increases the velocity of R e
at
.
810
O. P. Panda et al.
which have no catalytic activity but they support E
z
m in stability and solubility
(Edsall and Wyman 1958). Other factors which are associated in E
z
m activity are
cofactors metal ions and low molecular weight organic molecules i.e. co E
z
m . These
may be loosely or tightly bound by monovalent or covalent forces, contributing to
both E
z
m activity and stability (Morr and Ha 1993). E
z
m are named by adding the
suffix “-ase” to substrate e.g.; DNA polymerase E
z
m catalyzes polymerization of
nucleotides to form DNA (Gonzalez-Perez and Vereijken 2007). Urease E
z
m catalyzes urea hydrolysis, etc. Based on functions some E
z
m are also named e.g. pepsin
a digestive E
z
m , derived from Greek word Pepsis’ means digestion; lysozyme
responsible for cell wall lysis of bacteria (Ordonez et al. 2001). It derives some E
z
m
names from their source from where they are obtained, e.g. trypsin is produced by
pancreatic tissue after rubbing it with glycerin hence is named after Greek word
“tryein” meaning “to wear down”. As the time passes away, several new E
z
m are
discovered, some E
z
m have multiple names. To overcome these problems, they are
classified E
z
m based on the R e
at they catalyze after the international agreement
(Chandi and Sogi 2007). So, it classifies E
z
m according to the report of a
Nomenclature committee appointed by the International Union of Biochemistry. As
a result, all E
z
m get a formal E.C. (E
z
m Commission) number and some have their
trivial names (Hamada 2000). The E
z
m commission (EC) numbers divide E
z
m in
order to six major groups according to the R e
at catalyzed (Table 23.9).
23.6.2 Chemical Nature and Properties of E
z m
As discussed above, all E
z
m are p
R
t , and even it is found that it also acts on some
RNA molecules. Each E
z
m has its own specific structure and specific conformation,
which are essential things for catalytic activity (Garfin 2003). Holo E
z
m which
comprises of Apo E
z
m (the p
R
t part) and a co E
z
m (non- p
R
t organic part) is the
functional unit of the E
z
m . The non-p
R
t moiety, which is covalently bound with the
Apo E
z
m termed as prosthetic group, is the integral part of E
z
m structure. Dialysis
can separate the co E
z
m from the E
z
m , whereas they cannot separate the prosthetic
group (Aguilar 2004). If E
z
m is made up of a single poly P E
pt , it is referred as
monomeric E
z
m , if over one poly P E
pt chain present, known as oligomeric E
z
m , e.g.
lactate dehydrogenase. Multi E
z
m complexes possessing E
z
m have specific sites to
catalyze uncommon R e
at in a sequence. Some process can regulate E
z
m activity such
as phosphorylation, glycosylation. These processes alter the structure of a p
R
t found
in the E
z
m . It requires E
z
m in very minute quantity (Aguilar and Hearn 1996). It
does not absorb them in the overall E
z
m R e
at
, rather is received whole after completion of R e
at
. E
z
m do not alter the equilibrium constant (K) of a R e
at but only
increases the velocity of R e
at
.
810
O. P. Panda et al.