Fishmeal is being trusted as the most reliable protein source due to its nutritional quality in terms of attractability, palatability, digestibility, excellent nutrient profiles to fulfil the dietary requirement of aquatic species. The aquaculture sector consumes >70% of global fishmeal, though aqua feeds constitute only 4% in total industrial feed production (900-1,000 Mt in 2018). The global fishmeal production has shown a downward trend of 26.50% during 2000 to 2018 due to the occurrences of El Niño-Southern Oscillationsand other climatic events, which in turn increased the fishmeal price from 452 USD/t (2000) to 1596.54 USD/t (2018). The increasing trend of aquaculture production along with reduced fish-in/fish-out ratios (0.63 in 2000 to 0.33, 0.22 in 2010 and 2015 respectively) indicates the resilience of the aquafeed sector for fishmeal replacement. The wide availability, reasonable price and reliable nutrient content made an interest in plant protein sources, but their utilization was limited due to poor digestibility, imbalanced profiles of essential nutrients and the presence of anti-nutrients. Numerous methodologies are invented in recent times to enrich the nutritional qualities for maximizing the utilization of plant proteins in aquafeed formulations. The present review concludes that the aquafeed sector should use climate economics and technological innovations for substituting fishmeal to formulate the cost-effective feeds. K E Y W O R D Sclimate change, fermentation, fishmeal, input, output ratio, plant protein sources, shrimp feed
Acetylornithine aminotransferase (AcOAT) is one of the key enzymes involved in arginine metabolism and catalyzes the conversion of N-acetylglutamate semialdehyde to N-acetylornithine (AcOrn) in the presence of L-glutamate. It belongs to the Type I subgroup II family of pyridoxal 5'-phosphate (PLP) dependent enzymes. E. coli biosynthetic AcOAT (eAcOAT) also catalyzes the conversion of N-succinyl-L-2-amino-6-oxopimelate to N-succinyl-L,L-diaminopimelate, one of the steps in lysine biosynthesis. In view of the critical role of AcOAT in lysine and arginine biosynthesis, structural studies were initiated on the enzyme from S. typhimurium (sAcOAT). The K(m) and k(cat)/K(m) values determined with the purified sAcOAT suggested that the enzyme had much higher affinity for AcOrn than for ornithine (Orn) and was more efficient than eAcOAT. sAcOAT was inhibited by gabaculine (Gcn) with an inhibition constant (K(i)) of 7 microM and a second-order rate constant (k(2)) of 0.16 mM(-1) s(-1). sAcOAT, crystallized in the unliganded form and in the presence of Gcn or L-glutamate, diffracted to a maximum resolution of 1.90 A and contained a dimer in the asymmetric unit. The structure of unliganded sAcOAT showed significant electron density for PLP in only one of the subunits (subunit A). The asymmetry in PLP binding could be attributed to the ordering of the loop L(alphak-) (betam) in only one subunit (subunit B; the loop from subunit B comes close to the phosphate group of PLP in subunit A). Structural and spectral studies of sAcOAT with Gcn suggested that the enzyme might have a low affinity for PLP-Gcn complex. Comparison of sAcOAT with T. thermophilus AcOAT and human ornithine aminotransferase suggested that the higher specificity of sAcOAT towards AcOrn may not be due to specific changes in the active site residues but could result from minor conformational changes in some of them. This is the first structural report of AcOAT from a mesophilic organism and could serve as a basis for drug design as the enzyme is important for bacterial cell wall biosynthesis.
Serine hydroxymethyltransferase (SHMT) belongs to the a-family of pyridoxal 5¢-phosphate-dependent enzymes and catalyzes the reversible conversion of l-Ser and tetrahydrofolate to Gly and 5,10-methylene tetrahydrofolate. 5,10-Methylene tetrahydrofolate serves as a source of one-carbon fragment in many biological processes. SHMT also catalyzes the tetrahydrofolate-independent conversion of l-allo-Thr to Gly and acetaldehyde. The crystal structure of Bacillus stearothermophilus SHMT (bsSHMT) suggested that E53 interacts with the substrate, l-Ser and tetrahydrofolate. To elucidate the role of E53, it was mutated to Q and structural and biochemical studies were carried out with the mutant enzyme. The internal aldimine structure of E53QbsSHMT was similar to that of the wild-type enzyme, except for significant changes at Q53, Y60 and Y61. The carboxyl of Gly and side chain of l-Ser were in two conformations in the respective external aldimine structures. The mutant enzyme was completely inactive for tetrahydrofolate-dependent cleavage of l-Ser, whereas there was a 1.5-fold increase in the rate of tetrahydrofolate-independent reaction with l-allo-Thr. The results obtained from these studies suggest that E53 plays an essential role in tetrahydrofolate ⁄ 5-formyl tetrahydrofolate binding and in the proper positioning of Cb of l-Ser for direct attack by N5 of tetrahydrofolate. Most interestingly, the structure of the complex obtained by cocrystallization of E53QbsSHMT with Gly and 5-formyl tetrahydrofolate revealed the gem-diamine form of pyridoxal 5¢-phosphate bound to Gly and active site Lys. However, density for 5-formyl tetrahydrofolate was not observed. Gly carboxylate was in a single conformation, whereas pyridoxal 5¢-phosphate had two distinct conformations. The differences between the structures of this complex and Gly external aldimine suggest that the changes induced by initial binding of 5-formyl tetrahydrofolate are retained even though 5-formyl tetrahydrofolate is absent in the final structure. Spectral studies carried out with this mutant enzyme also suggest that 5-formyl tetrahydrofolate binds to the E53QbsSHMT-Gly complex forming a quinonoid intermediate and falls off Abbreviations
Serine hydroxymethyltransferase (SHMT) from Bacillus stearothermophilus (bsSHMT) is a pyridoxal 5′‐phosphate‐dependent enzyme that catalyses the conversion of l‐serine and tetrahydrofolate to glycine and 5,10‐methylene tetrahydrofolate. In addition, the enzyme catalyses the tetrahydrofolate‐independent cleavage of 3‐hydroxy amino acids and transamination. In this article, we have examined the mechanism of the tetrahydrofolate‐independent cleavage of 3‐hydroxy amino acids by SHMT. The three‐dimensional structure and biochemical properties of Y51F and Y61A bsSHMTs and their complexes with substrates, especially l‐allo‐Thr, show that the cleavage of 3‐hydroxy amino acids could proceed via Cα proton abstraction rather than hydroxyl proton removal. Both mutations result in a complete loss of tetrahydrofolate‐dependent and tetrahydrofolate‐independent activities. The mutation of Y51 to F strongly affects the binding of pyridoxal 5′‐phosphate, possibly as a consequence of a change in the orientation of the phenyl ring in Y51F bsSHMT. The mutant enzyme could be completely reconstituted with pyridoxal 5′‐phosphate. However, there was an alteration in the λmax value of the internal aldimine (396 nm), a decrease in the rate of reduction with NaCNBH3 and a loss of the intermediate in the interaction with methoxyamine (MA). The mutation of Y61 to A results in the loss of interaction with Cα and Cβ of the substrates. X‐Ray structure and visible CD studies show that the mutant is capable of forming an external aldimine. However, the formation of the quinonoid intermediate is hindered. It is suggested that Y61 is involved in the abstraction of the Cα proton from 3‐hydroxy amino acids. A new mechanism for the cleavage of 3‐hydroxy amino acids via Cα proton abstraction by SHMT is proposed.
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