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The three substrates of the enzymatic reaction are an L-amino acid, water, and oxygen, whereas the three products are the corresponding α-keto acid (2-oxo acid), ammonia, and hydrogen peroxide. One example of the enzyme in action occurs with the conversion L-alanine into pyruvic acid (2-oxopropanoic acid), as shown in Figure 1.
Snake venom is a highly toxic saliva [1] ... L-amino-acid oxidase, ... Spitting is a defensive reaction only. The snakes tend to aim for the eyes of a perceived threat.
(Left) The amino acid structure, (Middle) diagram and (Right) Stereodiagram of k-Bungarotoxin. [13] Evidence of early interest in snake venom was prevalent throughout the early 20th century with one of the first big breakthroughs being in the mid-1960s.
Glutamate can then be regenerated from α-KG via the action of transaminases or aminotransferase, which catalyze the transfer of an amino group from an amino acid to an α-keto acid. In this manner, an amino acid can transfer its amine group to glutamate, after which GDH can then liberate ammonia via oxidative deamination. This is a common ...
All three sarafotoxins are homologous peptides (four or less than four residue replacements) consisting of 21 amino acid residues. Their structure and activity are novel among snake venom components." [10] "The venom has a very high lethal potency, with an i.v. LD50 of 0.06-0.075 micrograms per g body weight in mice. The action of the venom is ...
An amine oxidase is an enzyme that catalyzes the oxidative cleavage of alkylamines into aldehydes and ammonia: [1] RCH 2 NH 2 + H 2 O + O 2 ⇌ {\displaystyle \rightleftharpoons } RCHO + NH 3 + H 2 O 2
One of the N. haje CRISPs was the first example of an acidic CRISP in reptilian venom. The selective ion channel activity of snake CRISPs, coupled with the variety of CRISPs available as the pool of venom proteins appears highly variable between (at least) cobra species, provide a valuable tool for probing the mechanisms of ion channel activity.
Fasciculin 1, Dendroaspis angusticeps (green mamba). Fasciculins are a class of toxic proteins found in certain snake venoms, notably some species of mamba.Investigations have revealed distinct forms in some green mamba venoms, in particular FAS1 and FAS2 [1] Fasciculins are so called because they cause intense fasciculation in muscle fascicles of susceptible organisms, such as the preferred ...