scholarly journals Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution

1992 ◽  
Vol 282 (3) ◽  
pp. 915-918 ◽  
Author(s):  
M P Jackman ◽  
M Huber ◽  
A Hajnal ◽  
K Lerch
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Amino Acid Substitution ◽  
Kinetic Properties ◽  
Binding Region ◽  
Invariant Residue ◽  
Streptomyces Glaucescens

Asp-208 of Streptomyces glaucescens tyrosinase (an invariant residue in the CuB-binding region of tyrosinases and haemocyanins) was conservatively substituted by glutamic acid. Although having little effect on spectroscopic or kinetic properties of the enzyme, the mutation greatly decreased the lability of Cu-bound O2. A rationalization for these results is given, based on the crystal structure of Panuliris interruptus haemocyanin in the conserved CuB-binding region.

scholarly journals A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria

Blood ◽  
1992 ◽  
Vol 79 (6) ◽  
pp. 1582-1585
Author(s):  
H Fujii ◽  
H Kanno ◽  
A Hirono ◽  
T Shiomura ◽  
S Miwa
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Messenger Rna ◽  
Phosphoglycerate Kinase ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Kinetic Properties ◽  
Total Blood ◽  
Single Nucleotide ◽  
Chronic Hemolysis

We have determined a single amino acid substitution in a new phosphoglycerate kinase (PGK) variant, PGK Shizuoka, associated with chronic hemolysis and myoglobinuria. PGK Shizuoka had an extremely low enzyme activity with normal kinetic properties and normal electrophoretic mobility. Total blood cell RNA of the patient was reverse-transcribed and amplified by the polymerase chain reaction. A single nucleotide substitution from guanine to thymine at position 473 of PGK messenger RNA was found. This nucleotide change causes a single amino acid substitution from Gly to Val at the 157th position, which is located in the NH2-terminal domain of the enzyme. This mutation creates a new Bst XI cleavage site in exon 5, and we thus confirmed the mutation in the variant gene. The replacement of Gly by Val is considered to affect enzyme catalysis.

scholarly journals Complexes between Nucleotide Base and Amino Acid. II. Crystal Structure of 5-Bromocytosine :N-Tosyl-L-glutamic Acid

1976 ◽  
Vol 49 (12) ◽  
pp. 3493-3497 ◽  
Author(s):  
Minoru Ohki ◽  
Akio Takenaka ◽  
Hirotaka Shimanouchi ◽  
Yoshio Sasada
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Nucleotide Base

scholarly journals Hemoglobin Genotypes Modulate Inflammatory Response to Plasmodium Infection

2020 ◽  
Vol 11 ◽  
Author(s):  
Keri Oxendine Harp ◽  
Felix Botchway ◽  
Yvonne Dei-Adomakoh ◽  
Michael D. Wilson ◽  
Joshua L. Hood ◽  
...  
Keyword(s):  
Amino Acid ◽  
Inflammatory Response ◽  
Glutamic Acid ◽  
Sickle Cell ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Inflammatory Factor ◽  
Hemoglobin S ◽  
Wide Range

In 2018, 228 million cases and 405,000 malaria-associated deaths were reported worldwide with a majority being in Africa. A wide range of factors, including parasitemia, host immunity, inflammatory responses to infection, and host hemoglobin genotype, mediate the severity of malaria. Among the hemoglobinopathies, hemoglobin S (HbS) is caused by a single amino acid substitution of Glutamic Acid replaced by Valine at the sixth position of the beta-globin chain (E6V). Hemoglobin C (HbC) on the other hand, involves a single amino acid substitution of Glutamic Acid by a Lysine (E6K), which has received the most attention. These substitutions alter the stability of Hb leading to wide-ranging hematological disorders. The homozygous state of hemoglobin S (HbSS) results in sickle cell anemia (SCA) whereas the heterozygous state (HbAS) results in sickle cell trait (SCT). Both mutations are reported to mediate the reduction in the severity and fatality of Plasmodium falciparum malaria. The mechanism underlying this protection is poorly understood. Since both malaria and sickle cell disease (SCD) are associated with the destruction of erythrocytes and widespread systemic inflammation, identifying which inflammatory factor(s) mediate susceptibility of individuals with different hemoglobin genotypes to Plasmodium infection could result in the discovery of new predictive markers and interventions against malaria or SCD severity. We hypothesized that hemoglobin genotypes modulate the inflammatory response to Plasmodium infection. We conducted a cross-sectional study in Ghana, West Africa, between 2014 and 2019 to ascertain the relationships between blood inflammatory cytokines, Plasmodium infection, and hemoglobin genotype. A total of 923 volunteers were enrolled in the study. A total of 74, age and sex-matched subjects were identified with various genotypes including HbAS, HbAC, HbSS, HbSC, HbCC, or HbAA. Complete blood counts and serum inflammatory cytokine expression levels were assessed. The results indicate that differential expression of CXCL10, TNF-α, CCL2, IL-8, and IL-6 were tightly linked to hemoglobin genotype and severity of Plasmodium infection and that these cytokine levels may be predictive for susceptibility to severe malaria or SCD severity.

scholarly journals A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria

Blood ◽  
1992 ◽  
Vol 79 (6) ◽  
pp. 1582-1585 ◽  
Author(s):  
H Fujii ◽  
H Kanno ◽  
A Hirono ◽  
T Shiomura ◽  
S Miwa
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Messenger Rna ◽  
Phosphoglycerate Kinase ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Kinetic Properties ◽  
Total Blood ◽  
Single Nucleotide ◽  
Chronic Hemolysis

Abstract We have determined a single amino acid substitution in a new phosphoglycerate kinase (PGK) variant, PGK Shizuoka, associated with chronic hemolysis and myoglobinuria. PGK Shizuoka had an extremely low enzyme activity with normal kinetic properties and normal electrophoretic mobility. Total blood cell RNA of the patient was reverse-transcribed and amplified by the polymerase chain reaction. A single nucleotide substitution from guanine to thymine at position 473 of PGK messenger RNA was found. This nucleotide change causes a single amino acid substitution from Gly to Val at the 157th position, which is located in the NH2-terminal domain of the enzyme. This mutation creates a new Bst XI cleavage site in exon 5, and we thus confirmed the mutation in the variant gene. The replacement of Gly by Val is considered to affect enzyme catalysis.

HYDROGEN-BONDED COMPLEX BETWEEN NUCLEOTIDE BASE AND AMINO ACID, CRYSTAL STRUCTURE OF 5-BROMOCYTOSINE:N-TOSYL-L-GLUTAMIC ACID

1974 ◽  
Vol 3 (6) ◽  
pp. 551-554
Author(s):  
Minoru Ohki ◽  
Akio Takenaka ◽  
Hirotaka Shimanouchi ◽  
Yoshio Sasada
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Acid Crystal ◽  
Nucleotide Base ◽  
Amino Acid Crystal ◽  
Hydrogen Bonded

Hubsm: A Novel Amino Acid Substitution Matrix for Comparing Hub Proteins

2017 ◽  
Vol 7 (8) ◽  
pp. 212
Author(s):  
Renganayaki G. ◽  
Achuthsankar S. Nair
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Low Complexity ◽  
Database Search ◽  
Substitution Matrix ◽  
Compositional Bias ◽  
Sequence Alignments ◽  
Amino Acid Substitution Matrix ◽  
Alignment Algorithms ◽  
Hub Proteins

Sequence alignment algorithms and  database search methods use BLOSUM and PAM substitution matrices constructed from general proteins. These de facto matrices are not optimal to align sequences accurately, for the proteins with markedly different compositional bias in the amino acid.   In this work, a new amino acid substitution matrix is calculated for the disorder and low complexity rich region of Hub proteins, based on residue characteristics. Insights into the amino acid background frequencies and the substitution scores obtained from the Hubsm unveils the  residue substitution patterns which differs from commonly used scoring matrices .When comparing the Hub protein sequences for detecting homologs,  the use of this Hubsm matrix yields better results than PAM and BLOSUM matrices. Usage of Hubsm matrix can be optimal in database search and for the construction of more accurate sequence alignments of Hub proteins.

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