Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Pyruvate kinase domain structures

Fig. 107. Pyruvate kinase domains 1, 2, and 3 as an example of a protein whose domains show no structural resemblance whatsoever. Fig. 107. Pyruvate kinase domains 1, 2, and 3 as an example of a protein whose domains show no structural resemblance whatsoever.
Figure 4.5 The polypeptide chain of the enzyme pyruvate kinase folds into several domains, one of which is an a/p barrel (red). One of the loop regions in this barrel domain is extended and comprises about 100 amino acid residues that fold into a separate domain (blue) built up from antiparallel P strands. The C-terminal region of about 140 residues forms a third domain (green), which is an open twisted a/p structure. Figure 4.5 The polypeptide chain of the enzyme pyruvate kinase folds into several domains, one of which is an a/p barrel (red). One of the loop regions in this barrel domain is extended and comprises about 100 amino acid residues that fold into a separate domain (blue) built up from antiparallel P strands. The C-terminal region of about 140 residues forms a third domain (green), which is an open twisted a/p structure.
Most of the antiparallel /3 domains have their sheets wrapped around into a cylinder, or barrel, shape. None of the antiparallel barrels has as symmetrical or as continuously hydrogen-bonded a cylindrical sheet as the singly wound parallel fi barrels of triosephos-phate isomerase and pyruvate kinase dl however, antiparallel barrels are very much more common. Because of gaps in the hydrogenbonding, some of these structures have been described as two /3 sheets facing each other (e.g., Schiffer et al., 1973 Blake et al., 1978 Harrison et al., 1978). Our reasons for treating them all as barrels are that the gap positions are sometimes different in domains that are probably related, and that the barrel description yields very much simpler and more unified topologies. [Pg.297]

Dephosphorylation of PEP and transfer of the phosphate to ADP catalyzed by pyruvate kinase is the last step in glycolysis. The structures of this enzyme from various species, bacteria and eukaryotes, are very similar. The catalytic domain of pyruvate kinase (Figure 15) has an overall structural feature of the TIM-fold barrel similar to the... [Pg.635]

Pyruvate Idnase deficiency (OMIM 266200) is the most common cause of nonspherocytic hemolytic anemia due to defective glycolysis. The allelic frequency is estimated to be around 2%. The consequent lack of sufficient energy, which is required for normal functioning and cellular survival, shortens the life span of the mature PK-deficient erythrocyte. Consequently, PK-deficient patients display a phenotype of nonspherocytic hemolytic anemia albeit with variable clinical severity. The clinical symptoms vary from neonatal death to a well-compensated hemolytic anemia. Patients benefit in general from a splenectomy. Pyruvate kinase deficiency is transmitted as an autosomal recessive disease. To date, more than 130 mutations in PKLR have been reported to be associated with pyruvate kinase deficiency (see Figure 21-10 for overview see reference 221). Most (70%) of these mutations are missense mutations affecting conserved residues in structurally and functionally important domains of PK. Splice site mutations, a deletion. [Pg.629]


See other pages where Pyruvate kinase domain structures is mentioned: [Pg.289]    [Pg.183]    [Pg.654]    [Pg.524]    [Pg.636]    [Pg.654]    [Pg.40]    [Pg.224]    [Pg.627]    [Pg.174]    [Pg.84]    [Pg.84]    [Pg.133]    [Pg.280]    [Pg.386]   
See also in sourсe #XX -- [ Pg.257 , Pg.258 , Pg.264 , Pg.267 , Pg.270 , Pg.281 , Pg.294 , Pg.297 , Pg.300 , Pg.314 , Pg.316 ]




SEARCH



Domain structure

Kinase domain

Kinase structures

Kinases pyruvate kinase

Pyruvate kinase

Structural domains

© 2024 chempedia.info