STRUCTURAL INSIGHTS INTO NOVEL MICROBIAL METALLOENZYMES
... Metalloproteins represent a large portion of the total proteome. When bound to a protein a metal ion influences both protein stability and function through structural, catalytic or regulatory roles. Discovery of a metal ion cofactor presents new insight into both the structural and functional aspect ...
... Metalloproteins represent a large portion of the total proteome. When bound to a protein a metal ion influences both protein stability and function through structural, catalytic or regulatory roles. Discovery of a metal ion cofactor presents new insight into both the structural and functional aspect ...
amino acids
... to the presence of hydroxyl groups, sulfur atoms or amide groups which may form hydrogen bonds with water. ...
... to the presence of hydroxyl groups, sulfur atoms or amide groups which may form hydrogen bonds with water. ...
Chapter 3: Amino Acids and Peptides
... General Structure of an Amino Acid The twenty α-amino acids that are encoded by the genetic code share the generic structure, differing only at the R substituent, except for one amino acid ...
... General Structure of an Amino Acid The twenty α-amino acids that are encoded by the genetic code share the generic structure, differing only at the R substituent, except for one amino acid ...
2. Genetic code is degenerate（简并性）
... 9 hydrogen bones (tertiary hydrogen bones) to help the formation of tRNA tertiary structure, mainly involving in the base paring between the invariant bases. ...
... 9 hydrogen bones (tertiary hydrogen bones) to help the formation of tRNA tertiary structure, mainly involving in the base paring between the invariant bases. ...
AAlast+nuc
... Most amino acid degradations begin with transaminations to make glutamate; the resulting alpha-keto acids are further metabolized ...
... Most amino acid degradations begin with transaminations to make glutamate; the resulting alpha-keto acids are further metabolized ...
Regulation of the Citric Acid Cycle
... The enzyme has a covalently bound biotin cofactor. Since this enzyme functions in gluconeogenesis, it is allosterically regulated. This enzyme requires acetyl-CoA to be bound at an allosteric binding site in order to activate bicarbonate with ATP. PEP carboxylase is found in yeast, bacteria and plan ...
... The enzyme has a covalently bound biotin cofactor. Since this enzyme functions in gluconeogenesis, it is allosterically regulated. This enzyme requires acetyl-CoA to be bound at an allosteric binding site in order to activate bicarbonate with ATP. PEP carboxylase is found in yeast, bacteria and plan ...
Nucleotides: Synthesis and Degradation
... Explore dUTPase as follows: • Find the substrate in its binding site • Find C5 on the Uracil group. Is there enough room to attach a methyl group to C5? • Locate the ribose 2’ C. What protein group sterically prevents an –OH group from being attached to the 2’ C atom? • Find the H-bond donors and ac ...
... Explore dUTPase as follows: • Find the substrate in its binding site • Find C5 on the Uracil group. Is there enough room to attach a methyl group to C5? • Locate the ribose 2’ C. What protein group sterically prevents an –OH group from being attached to the 2’ C atom? • Find the H-bond donors and ac ...
Carbamoyl phosphate synthetase - Department of Biochemistry
... [24°°]. A close-up view of the region surrounding the intermediate is shown in Figure 6. T h e hydroxyl group of Ser47 and the backbone amide hydrogen of Gly-241 are in ideal locations to position the carbonyl carbon atom of the substrate for nucleophilic attack by the thiolate anion of Cys269 and t ...
... [24°°]. A close-up view of the region surrounding the intermediate is shown in Figure 6. T h e hydroxyl group of Ser47 and the backbone amide hydrogen of Gly-241 are in ideal locations to position the carbonyl carbon atom of the substrate for nucleophilic attack by the thiolate anion of Cys269 and t ...
Document
... amphibolic intermediates used as sources of energy or for carbohydrate and lipid biosynthesis. • Initial reaction • Transamination • Remove any additional nitrogen ...
... amphibolic intermediates used as sources of energy or for carbohydrate and lipid biosynthesis. • Initial reaction • Transamination • Remove any additional nitrogen ...
MedicalBiochemistry
... polypeptide. Figure I.5 shows the analysis of a polypeptide hydrolysate by ion exchange chromatography. Note that during hydrolysis, the side-chain amides of asparagine and glutamine are hydrolyzed and these amino acids are detected as glutamic acid and aspartic acid. For each glutamine or asparagin ...
... polypeptide. Figure I.5 shows the analysis of a polypeptide hydrolysate by ion exchange chromatography. Note that during hydrolysis, the side-chain amides of asparagine and glutamine are hydrolyzed and these amino acids are detected as glutamic acid and aspartic acid. For each glutamine or asparagin ...
The Three-dimensional Structure of 4-Hydroxybenzoyl
... b-hydroxydecanoyl thiol ester dehydrase from Escherichia coli (15). By superimposing the two structures, it has been possible to identify the probable active site region of the thioesterase and to propose a catalytic mechanism whereby the carboxylate side chain of Asp17 activates a water molecule fo ...
... b-hydroxydecanoyl thiol ester dehydrase from Escherichia coli (15). By superimposing the two structures, it has been possible to identify the probable active site region of the thioesterase and to propose a catalytic mechanism whereby the carboxylate side chain of Asp17 activates a water molecule fo ...
Review of Analytical Methods Part 1: Spectrophotometry
... • Binding of BCG and BCP is not specific, since other proteins have Asp and Glu residues – Reading absorbance within 30 s improves specificity ...
... • Binding of BCG and BCP is not specific, since other proteins have Asp and Glu residues – Reading absorbance within 30 s improves specificity ...
Saimaa University of Applied Sciences Faculty of Technology, Imatra, Finland ’s Degree Bachelor
... Enzymes are giant macromolecules, biological catalysts and they mostly consisted of protein, which are polymers of amino acids and small amount of RNA. The molecular weight of enzyme is from 10,000 to 2000,000 Da. All enzymes contain four elements C, H, O, N. In the organisms, synthesis and degradat ...
... Enzymes are giant macromolecules, biological catalysts and they mostly consisted of protein, which are polymers of amino acids and small amount of RNA. The molecular weight of enzyme is from 10,000 to 2000,000 Da. All enzymes contain four elements C, H, O, N. In the organisms, synthesis and degradat ...
Catalytic triad
A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.