enzyme deficiency
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2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Phonchanan Pakparnich ◽  
Sirapapha Sudsumrit ◽  
Mallika Imwong ◽  
Teeraporn Suteewong ◽  
Kamonwan Chamchoy ◽  
...  

AbstractGlucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common enzymopathy in humans, affecting ~ 500 million worldwide. A detailed study of the structural stability and catalytic activity of G6PD variants is required to understand how different mutations cause varying degrees of enzyme deficiency, reflecting the response of G6PD variants to oxidative stress. Furthermore, for G6PD double variants, investigating how two mutations jointly cause severe enzyme deficiency is important. Here, we characterized the functional and structural properties of nine G6PD variants: G6PD Gaohe, G6PD Mahidol, G6PD Shoklo, G6PD Canton, G6PD Kaiping, G6PD Gaohe + Kaiping, G6PD Mahidol + Canton, G6PD Mahidol + Kaiping and G6PD Canton + Kaiping. All variants were less catalytically active and structurally stable than the wild type enzyme, with G6PD double mutations having a greater impact than single mutations. G6PD Shoklo and G6PD Canton + Kaiping were the least catalytically active single and double variants, respectively. The combined effects of two mutations were observed, with the Canton mutation reducing structural stability and the Kaiping mutation increasing it in the double mutations. Severe enzyme deficiency in the double mutants was mainly determined by the trade-off between protein stability and catalytic activity. Additionally, it was demonstrated that AG1, a G6PD activator, only marginally increased G6PD enzymatic activity and stability.


Endocrine ◽  
2021 ◽  
Author(s):  
Aslı Beştaş ◽  
Semih Bolu ◽  
Edip Unal ◽  
Amine Aktar Karakaya ◽  
Recep Eröz ◽  
...  

Author(s):  
Melis Ulak Ozkan ◽  
Selahattin Katar ◽  
Edibe Pembegul Yildiz ◽  
Nur Aydinli ◽  
Mine Caliskan

2021 ◽  
Vol 49 (2) ◽  
pp. 157
Author(s):  
R. Dewasurendra ◽  
N. Sepulveda ◽  
N. Chandrasekharan ◽  
N. Karunaweera ◽  
S. Gunawardena

Author(s):  
Abdurrahman Akgun ◽  
Askin Sen ◽  
Hasan Onal

Abstract Objectives Hypotonia, lethargy, eczema, alopecia, conjunctivitis, ataxia, hearing loss, optic atrophy, cognitive retardation, and seizures can occur in patients with biotinidase deficiency, and it is inherited as autosomal recessive. The aim of this study was to evaluate the cases followed up with the diagnosis of biotinidase deficiency in our unit, in terms of clinical, biochemical and genetic analyses. Methods A total of 112 cases followed up in our centre with the diagnosis of biotinidase deficiency between August 2018–September 2020 were included in the study. Data were collected retrospectively. Results A total of 112 cases (55.4% male, mean age: 2.2 ± 2.8 years) diagnosed with biotinidase deficiency were evaluated. Diagnoses were made by newborn screening in 90.2% of the cases, by family screening in 4.5%, and by investigating symptoms in 5.4%. The most frequently (27.5%) detected mutations were c.1330G>C (p.D444H)/c.1330G>C (p.D444H) homozygous mutation, followed by (13.0%) c.1330G>C (p.D444H)/c.470G>A (p.R157H) compound heterozygous mutation, and (13.0%) c.470G>A (p.R157H)/c.470G>A (p.R157H) homozygous mutation. Biotinidase enzyme levels were found to be higher in patients with the p.D444H homozygous mutation than patients with other mutations. Biotin treatment was started in all patients with enzyme deficiency. Conclusions Since the treatment is inexpensive and easily available, it is vital to detect this disease before symptom onset, especially findings related to the central nervous system, hearing and vision loss. In patients diagnosed with enzyme deficiency, the diagnosis should be definitively confirmed by genetic analysis.


Author(s):  
Juliano Henrique Borges ◽  
Daniel Minutti de Oliveira ◽  
Sofia Helena Valente de Lemos-Marini ◽  
Bruno Geloneze ◽  
Gil Guerra-Júnior ◽  
...  

2021 ◽  
Author(s):  
Anuradha Deorukhkar ◽  
Anuja KULKARNI ◽  
Prabhakar S Kedar

Abstract Two types of recessive congenital methaemoglobinemia (RCM) is caused by NADH-dependent cytochrome b5 reductase enzyme deficiency encoded by CYB5R3 gene. RCM-I is characterized by higher methaemoglobin levels (>2 g/dL), causing only cyanosis, whereas RCMR-II is associated with cyanosis with neurological impairment. The present study discovered three novel homozygous pathogenic variants of CYB5R3 causing RCM I and II in four unrelated Indian patients. In patient-1 and patient-2 of are of RCM type I caused due to novel c.175C>T (p.Arg59Cys) and other reported c.469T>C (p.Phe157Ser) missense pathogenic variants respectively, whereas patient-3 and patient-4 presented with the RCM type II are related to developmental delay with cyanosis since birth due to a novel homozygous (g.25679_25679delA) splice-site deletion and novel homozygous c.824_825insC (p.Pro278ThrfsTer367) single nucleotide insertion. The CYB5R3 transcript levels were estimated by qRT-PCR in the splice-site deletion, which was 0.33fold of normal healthy control. The insertion of nucleotide C resulted in a frame-shift of termination codon are associated with neurological impairment. This study can help to conduct genetic counselling and, subsequently, prenatal diagnosis of high-risk genetic disorders.


Biochimie ◽  
2021 ◽  
Vol 186 ◽  
pp. 28-32
Author(s):  
Dominika Malinska ◽  
Giorgia Testoni ◽  
Malgorzata Bejtka ◽  
Jordi Duran ◽  
Joan J. Guinovart ◽  
...  

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