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alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
D-fructose 6-phosphate + NH3
alpha-D-glucosamine 6-phosphate + H2O
-
-
-
-
r
D-fructose 6-phosphate + NH3
D-glucosamine 6-phosphate + H2O
-
deamination reaction is preferred over amination/isomerization
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
additional information
?
-
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
in standard culture conditions keratinocyte GNPDAs mainly catalyze the reaction from GlcN6P back to Fru6P
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
specific for
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
active towards alpha-anomer, inactive towards the beta-anomer. Strong affinity for the open-chain form of glucosamine 6-phosphate
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
no indication of reversibility is noted
-
ir
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
deamination reaction is preferred over amination/isomerization
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
?
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
?
additional information
?
-
-
the enzyme catalyses the first commited step in a biosynthetic pathway leading to amino sugar-nucleotide precursor of bacterial peptidoglycan
-
-
?
additional information
?
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview
-
-
-
additional information
?
-
-
the activity of the enzyme in erythrocytes is low, indicating that hexosamine catabolism is not a major source of energy in the erythrocyte
-
-
?
additional information
?
-
-
enzyme in spermatozoa may play a role during the acrosome reaction
-
-
?
additional information
?
-
kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+
-
-
-
additional information
?
-
kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+
-
-
-
additional information
?
-
kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
D-fructose 6-phosphate + NH3
alpha-D-glucosamine 6-phosphate + H2O
-
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
additional information
?
-
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
in standard culture conditions keratinocyte GNPDAs mainly catalyze the reaction from GlcN6P back to Fru6P
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
?
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
?
additional information
?
-
-
the enzyme catalyses the first commited step in a biosynthetic pathway leading to amino sugar-nucleotide precursor of bacterial peptidoglycan
-
-
?
additional information
?
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview
-
-
-
additional information
?
-
-
the activity of the enzyme in erythrocytes is low, indicating that hexosamine catabolism is not a major source of energy in the erythrocyte
-
-
?
additional information
?
-
-
enzyme in spermatozoa may play a role during the acrosome reaction
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-deoxyglucose 6-phosphate
-
activates
6-phosphogluconate
-
activates
D-mannose 6-phosphate
-
-
GlcNAc6P
enzyme NagB is allosterically activated by GlcNAc6P
N-acetylgalactosamine
-
-
N-Acetylgalactosamine 6-phosphate
-
activates
N-acetylglucosamine 6-phosphate
N-acetylglucosamine-6-phosphate
-
allosteric activator of NagB
PCMB
-
inhibits at high concentrations, activates at low concentrations
UDP-N-acetylglucosamine
-
slight activation at 0.00167-0.167 mM, slight inhibition at 1.67 mM
D-glucose 6-phosphate
-
activates
D-glucose 6-phosphate
-
activates
N-acetylglucosamine 6-phosphate
-
activator of the enzyme in amination direction, leads to about 30% increased activity at 0.07-0.14 mM, overview
N-acetylglucosamine 6-phosphate
-
activates enzyme by increasing its kcat without any change in the Km values for D-glucosamine 6-phosphate
N-acetylglucosamine 6-phosphate
-
the cooperativity of the reaction is completely abolished by saturating concentrations of GlcNAcGP, this allosteric modulator activated the reaction with a typical K-effect, overview
N-acetylglucosamine 6-phosphate
-
-
N-acetylglucosamine 6-phosphate
-
N-acetylglucosamine 6-phosphate
-
-
N-acetylglucosamine 6-phosphate
-
activates
N-acetylglucosamine 6-phosphate
-
increases reaction velocity when D-glucosamine 6-phosphate is present at levels below that required for saturation
N-acetylglucosamine 6-phosphate
GlcNAc6P, allosteric site ligand, behaving as a V activator and a K inhibitor: in the absence of GlcNAc6P, the apparent kcat of the enzyme is so low, that GlcNAc6P behaves as an essential activator. Additionally, substrate inhibition, dependent on GlcNAc6P concentration, is observed, Monod allosteric model with some additional postulates, overview. The ligand binds to either enzyme conformational state, but with higher affinity for the R form
N-acetylglucosamine 6-phosphate
-
activates
N-acetylglucosamine 6-phosphate
-
activates in both directions
N-acetylglucosamine 6-phosphate
-
activates
additional information
-
no effect by glucose 6-phosphate
-
additional information
-
enzyme contains 5 half-cystines per monomer, the sulfhydryls are not essential for catalysis or allosteric behavior of the enzyme
-
additional information
-
each subunit has for Cys residues located at positions 118, 219, 228 and 239, Cys118 and Cys239 form a pair of vicinal thiols
-
additional information
NanE, GlcNAc-6P epimerase, and the uridylylated PII protein allosterically activate NagB by direct protein-protein interactions, overview. Uridylylated PII (but not underivatized PII) activates NagB about 10fold at low concentrations of substrate, whereas NanE increases NagB activity about 2fold. NanE activates NagB in the absence or presence of GlcNAc-6P, but histidine-phosphorylatable phosphocarrier protein (HPr) and U-PII activation requires the presence of GlcNAc-6P. NanE-dependent activation of NagB is not dependent on GlcNAc-6P. Activation of NagB by HPr and uridylylated PII, as well as by NanE and HPr (but not by NanE and U-PII), is synergistic, and the modeling, which suggests specific residues involved in complex formation, provides possible explanations. The uridylylated PII protein (U-PII) is generated by posttranslational modification under nitrogen-limiting conditions involving the glutamine/2-oxoglutarate ratio-sensing uridylyltransferase/uridylyl-removing enzyme GlnD. PII (GlnB)-dependent activation of NagB depends on the uridylylation state of GlnB, kinetics for NagB in the presence of PII at different stages of PII modification involving uridylylation by GlnD, overview. The effect is greater at pH 7.5 than at pH 8 due to the allosteric behavior of the Ser-1 mutant NagB, resulting from an increased Hill coefficient, also noticed for the wild-type NagB. Modeling of HPr/U-PII and of HPr/NanE binding to NagB. The PII protein is known to be a regulator of both the activity and the synthesis of glutamine synthetase (GlnA) in enteric bacteria, and of nitrogen metabolism in many other bacteria, archaea, and eukaryotes, in response to the availability of nitrogen sources
-
additional information
-
enzyme activity is not modified by GlcNAc6P, UDPGlcNAc, or UDP-GalNAc
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Asthma
Analyses of shared genetic factors between asthma and obesity in children.
Asthma
Obese individuals experience wheezing without asthma but not asthma without wheezing: a Mendelian randomisation study of 85?437 adults from the Copenhagen General Population Study.
Candidiasis
Attenuation of virulence and changes in morphology in Candida albicans by disruption of the N-acetylglucosamine catabolic pathway.
Carcinoma, Hepatocellular
Erratum: Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma [Corrigendum].
Carcinoma, Hepatocellular
Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma.
Colorectal Neoplasms
Identification of differential proteins in colorectal cancer cells treated with caffeic acid phenethyl ester.
Colorectal Neoplasms
Susceptibility variants for obesity and colorectal cancer risk: The multiethnic cohort and PAGE studies.
Cysts
Developmental gene regulation in Giardia lamblia: first evidence for an encystation-specific promoter and differential 5' mRNA processing.
Cysts
Proteomic Study of Entamoeba histolytica Trophozoites, Cysts, and Cyst-Like Structures.
Diabetes Mellitus, Type 2
A Perception on Genome-Wide Genetic Analysis of Metabolic Traits in Arab Populations.
Diabetes Mellitus, Type 2
Implication of genetic variants near NEGR1, SEC16B, TMEM18, ETV5/DGKG, GNPDA2, LIN7C/BDNF, MTCH2, BCDIN3D/FAIM2, SH2B1, FTO, MC4R, and KCTD15 with obesity and type 2 diabetes in 7705 Chinese.
Diabetes Mellitus, Type 2
Obesity-related genomic loci are associated with type 2 diabetes in a Han Chinese population.
Diabetes Mellitus, Type 2
Obesity-related loci in TMEM18, CDKAL1 and FAIM2 are associated with obesity and type 2 diabetes in Chinese Han patients.
Diabetes Mellitus, Type 2
Sexual Dimorphism of a Genetic Risk Score for Obesity and Related Traits among Chinese Patients with Type 2 Diabetes.
Fibrosarcoma
Association between obesity and polymorphisms in SEC16B, TMEM18, GNPDA2, BDNF, FAIM2 and MC4R in a Japanese population.
Insulin Resistance
Contribution of 24 obesity-associated genetic variants to insulin resistance, pancreatic beta-cell function and type 2 diabetes risk in the French population.
Neoplasm Metastasis
Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma.
Neoplasms
Erratum: Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma [Corrigendum].
Neoplasms
Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma.
Neoplasms
Prognostic value of a novel glycolysis-related gene expression signature for gastrointestinal cancer in the Asian population.
Niemann-Pick Diseases
Association between obesity and polymorphisms in SEC16B, TMEM18, GNPDA2, BDNF, FAIM2 and MC4R in a Japanese population.
Obesity
Analysis of the contribution of FTO, NPC1, ENPP1, NEGR1, GNPDA2 and MC4R genes to obesity in Mexican children.
Obesity
Association between obesity and polymorphisms in SEC16B, TMEM18, GNPDA2, BDNF, FAIM2 and MC4R in a Japanese population.
Obesity
Association of genetic variants for susceptibility to obesity with type 2 diabetes in Japanese individuals.
Obesity
Association of variations in the FTO, SCG3 and MTMR9 genes with metabolic syndrome in a Japanese population.
Obesity
Associations of six single nucleotide polymorphisms in obesity-related genes with body mass index and risk of obesity in the Chinese children.
Obesity
Characterizing gene-gene interactions in a statistical epistasis network of twelve candidate genes for obesity.
Obesity
Effect of 15 BMI-Associated Polymorphisms, Reported for Europeans, across Ethnicities and Degrees of Amerindian Ancestry in Mexican Children.
Obesity
Environment and Gene Association With Obesity and Their Impact on Neurodegenerative and Neurodevelopmental Diseases.
Obesity
Exome sequencing in Thai patients with familial obesity.
Obesity
Genetic susceptibility, birth weight and obesity risk in young Chinese.
Obesity
GNPDA2 Gene Affects Adipogenesis and Alters the Transcriptome Profile of Human Adipose-Derived Mesenchymal Stem Cells.
Obesity
Identification, expression and variation of the GNPDA2 gene, and its association with body weight and fatness traits in chicken.
Obesity
Implication of genetic variants near NEGR1, SEC16B, TMEM18, ETV5/DGKG, GNPDA2, LIN7C/BDNF, MTCH2, BCDIN3D/FAIM2, SH2B1, FTO, MC4R, and KCTD15 with obesity and type 2 diabetes in 7705 Chinese.
Obesity
Obesity susceptibility loci in Qataris, a highly consanguineous Arabian population.
Obesity
Obesity-related genes are expressed in human Sertoli cells and modulated by energy homeostasis regulating hormones.
Obesity
Obesity-related genomic loci are associated with type 2 diabetes in a Han Chinese population.
Obesity
Obesity-related loci in TMEM18, CDKAL1 and FAIM2 are associated with obesity and type 2 diabetes in Chinese Han patients.
Obesity
Protective Association of Single Nucleotide Polymorphisms rs1861868-FTO and rs7975232-VDR and Obesity in Saudi Females.
Obesity
Replication and extension of genome-wide association study results for obesity in 4923 adults from northern Sweden.
Obesity
Replication of 13 obesity loci among Singaporean Chinese, Malay and Asian-Indian populations.
Obesity
Sexual Dimorphism of a Genetic Risk Score for Obesity and Related Traits among Chinese Patients with Type 2 Diabetes.
Obesity
Study of eight GWAS-identified common variants for association with obesity-related indices in Chinese children at puberty.
Obesity
The current review of adolescent obesity: the role of genetic factors.
Obesity
The Influence of Obesity-Related Single Nucleotide Polymorphisms on BMI Across the Life Course: The PAGE Study.
Obesity
The Relationships of Obesity-Related Genetic Variants With Metabolic Profiles and Response to Metformin in Clozapine-Treated Patients With Schizophrenia.
Obesity
Validation of BMI genetic risk score and DNA methylation in a Korean population.
Obesity
What model organisms and interactomics can reveal about the genetics of human obesity.
Pediatric Obesity
Genome-wide association analysis identifies three new susceptibility loci for childhood body mass index.
Pediatric Obesity
Role of BMI-Associated Loci Identified in GWAS Meta-Analyses in the Context of Common Childhood Obesity in European Americans.
Synucleinopathies
Deployment of Label-Free Quantitative Olfactory Proteomics to Detect Cerebrospinal Fluid Biomarker Candidates in Synucleinopathies.
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0.24 - 45.2
alpha-D-glucosamine 6-phosphate
1.1 - 36
D-fructose 6-phosphate
0.041 - 17
D-glucosamine 6-phosphate
1.7
fructose 6-phosphate
-
amination reaction, pH 8.0, 30°C
5
glucosamine 6-phosphate
-
deamination reaction, pH 8.0, 30°C
additional information
additional information
-
0.24
alpha-D-glucosamine 6-phosphate
pH 8.0, 20°C, recombinant enzyme
0.85
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
1.21
alpha-D-glucosamine 6-phosphate
-
HisC-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
1.5
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
1.9
alpha-D-glucosamine 6-phosphate
pH 6.8, 30°C, 0.2 mM GlcNAc-6P, enzyme in absence of NanE
2
alpha-D-glucosamine 6-phosphate
pH 6.8, 30°C, 0.2 mM GlcNAc-6P, enzyme in presence of NanE
2.3
alpha-D-glucosamine 6-phosphate
pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in presence of PII protein
2.9
alpha-D-glucosamine 6-phosphate
pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in absence of PII protein
3.6
alpha-D-glucosamine 6-phosphate
pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in presence of uridylylated PII protein
38.1
alpha-D-glucosamine 6-phosphate
-
untagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
45.2
alpha-D-glucosamine 6-phosphate
-
HisN-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
1.1
D-fructose 6-phosphate
-
pH 7.3, 60°C
1.7
D-fructose 6-phosphate
-
pH 7.7, 30°C, in presence of 0.5 mM N-acetylglucosamine 6-phosphate
1.71
D-fructose 6-phosphate
-
HisN-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
2.5
D-fructose 6-phosphate
-
pH 8.9, 30°C
2.8
D-fructose 6-phosphate
-
untagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
3.5
D-fructose 6-phosphate
-
pH 8.5, 37°C, in presence of N-acetylglucosamine 6-phosphate and Mn2+
3.52
D-fructose 6-phosphate
-
HisC-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
4.8
D-fructose 6-phosphate
-
pH 8.5, 37°C, in presence of 10 mM glucose 6-phosphate
5.5
D-fructose 6-phosphate
-
pH 8.2, 37°C, in presence of N-acetylglucosamine 6-phosphate
5.9
D-fructose 6-phosphate
-
pH 7.5, 30°C
6
D-fructose 6-phosphate
-
pH 6.8, 39°C
22.5
D-fructose 6-phosphate
-
pH 8.5, 37°C, in absence of activators
33
D-fructose 6-phosphate
-
pH 8.2, 37°C, in absence of activator
36
D-fructose 6-phosphate
-
pH 8.5, 37°C, in absence of activators
0.041
D-glucosamine 6-phosphate
-
pH 9, 37°C
0.1
D-glucosamine 6-phosphate
-
pH 7.5, 37°C
0.13
D-glucosamine 6-phosphate
-
22°C, pH 8.0
0.25
D-glucosamine 6-phosphate
-
pH 8.5, 37°C, in presence of N-acetylglucosamine 6-phosphate and Mn2+
0.25
D-glucosamine 6-phosphate
-
pH 8.2, 37°C, in presence of N-acetylglucosamine 6-phosphate and Mn2+
0.25
D-glucosamine 6-phosphate
-
hyperbolic kinetic conditions, in presence of 1 mM N-acetylglucosamine 6-phosphate, pH 8.8
0.26
D-glucosamine 6-phosphate
mutant W15Y/W224Y/Y254W, pH 7.5, S0.5-value 0.5 mM
0.27
D-glucosamine 6-phosphate
recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 1, in absence of N-acetylglucosamine 6-phosphate
0.33
D-glucosamine 6-phosphate
mutant R172A/K208E, Michaelis-Hill equation
0.339
D-glucosamine 6-phosphate
-
pH 7.3, 60°C
0.38
D-glucosamine 6-phosphate
-
pH 6.82, 39°C
0.4
D-glucosamine 6-phosphate
-
pH 7.8, 25°C
0.46
D-glucosamine 6-phosphate
mutant C118S/C228S/C239S, pH 7.5, 30°C
0.49
D-glucosamine 6-phosphate
mutant W15Y/F174W/W224Y, pH 7.5, S0.5-value 3.4 mM
0.49
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C206, pH 7.5, 30°C
0.5
D-glucosamine 6-phosphate
mutant W224Y, pH 7.5, S0.5-value 4.8 mM
0.5
D-glucosamine 6-phosphate
wild-type, pH 7.5, 30°C
0.51
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C
0.52
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C
0.52
D-glucosamine 6-phosphate
wild-type, modified with bimane at C206, pH 7.5, 30°C
0.55
D-glucosamine 6-phosphate
-
pH 7.5, 30°C, wild-type enzyme, in presence of N-acetylglucosamine 6-phosphate
0.55
D-glucosamine 6-phosphate
wild-type, Michaelis-Hill equation
0.55
D-glucosamine 6-phosphate
wild-type, pH 7.5, S0.5-value 5.5 mM
0.61
D-glucosamine 6-phosphate
mutant K208E, Michaelis-Hill equation
0.62
D-glucosamine 6-phosphate
mutant W15Y, pH 7.5, S0.5-value 5.8 mM
0.65
D-glucosamine 6-phosphate
-
pH 8.0, 30°C
0.65
D-glucosamine 6-phosphate
mutant W15Y/W224Y, pH 7.5, S0.5-value 5.0 mM
0.66
D-glucosamine 6-phosphate
-
pH 7.9, 37°C, activated by N-acetylglucosamine 6-phosphate
0.67
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, mutant enzyme Tyr121Trp
0.69
D-glucosamine 6-phosphate
mutant K208V, Michaelis-Hill equation
1.1
D-glucosamine 6-phosphate
-
pH 8.2, 37°C, without activator
1.2
D-glucosamine 6-phosphate
-
pH 7.8, 37°C, activated by N-acetylglucosamine 6-phosphate
1.67
D-glucosamine 6-phosphate
mutant R172A, Michaelis-Hill equation
2
D-glucosamine 6-phosphate
recombinant isozyme GNPDA1 275 truncation mutant, pH 8.0, 30°C, kinetic method 1
2.01
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, wild-type enzyme
2.2
D-glucosamine 6-phosphate
-
in presence of 0.2 mM N-acetylglucosamine 6-phosphate
2.37
D-glucosamine 6-phosphate
-
pH 8.5, 37°C, without activator
2.6
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, mutant enzyme Tyr121Thr
3.43
D-glucosamine 6-phosphate
-
pH 7.5, 30°C, mutant F174A, in presence of N-acetylglucosamine 6-phosphate
4.6
D-glucosamine 6-phosphate
wild-type, modified with bimane at C206, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.1
D-glucosamine 6-phosphate
mutant C118S/C228S/C239S, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.1
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.1
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C206, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.2
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
5.2
D-glucosamine 6-phosphate
wild-type, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator
7.1
D-glucosamine 6-phosphate
-
pH 7.8, 37°C
9
D-glucosamine 6-phosphate
-
pH 7.5, 37°C
12.5
D-glucosamine 6-phosphate
-
pH 7.2
14
D-glucosamine 6-phosphate
-
pH 7.8, 37°C, without activator
16.5
D-glucosamine 6-phosphate
recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 1, in presence of saturating concentration of N-acetylglucosamine 6-phosphate
17
D-glucosamine 6-phosphate
-
pH 8.5, 37°C, in absence of activators, or in presence of glucose 6-phosphate
2 - 3
NH3
-
untagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
14
NH3
-
HisN-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
41.6
NH3
-
HisC-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C
3.7
NH4+
-
pH 7.5, 30°C
4.2
NH4+
-
pH 8.5, 37°C, in presence of glucose 6-phosphate
16
NH4+
-
pH 8.5, 37°C, in presence of N-acetylglucosamine 6-phosphate and Mn2+
25
NH4+
-
in absence of activators
31.4
NH4+
-
pH 7.7, 30°C, in presence of 0.25 mM N-acetylglucosamine 6-phosphate
35.4
NH4+
-
pH 7.7, 30°C, without activator
43
NH4+
-
pH 8.2, 37°C, in presence of N-acetylglucosamine 6-phosphate
300
NH4+
-
pH 8.2, 37°C, without activator
additional information
additional information
comparison of KM of unmodified and N-terminal modified enzyme
-
additional information
additional information
-
comparison of KM of unmodified and N-terminal modified enzyme
-
additional information
additional information
comparison of KM of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
-
comparison of KM of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
-
no homotropic allosteric properties
-
additional information
additional information
-
the enzyme displays positive homotropic cooperativity towards D-glucosamine 6-phosphate
-
additional information
additional information
allosteric enzyme, hGNPDA1 enzyme displays hyperbolic kinetics but very low-activity in the absence of GlcNAc6P, kinetic analysis and modelling of both reaction directions, detailed overview
-
additional information
additional information
allosteric enzyme, hGNPDA1 enzyme displays hyperbolic kinetics but very low-activity in the absence of GlcNAc6P, kinetic analysis and modelling of both reaction directions, detailed overview
-
additional information
additional information
-
allosteric enzyme, hGNPDA1 enzyme displays hyperbolic kinetics but very low-activity in the absence of GlcNAc6P, kinetic analysis and modelling of both reaction directions, detailed overview
-
additional information
additional information
allosterically regulated enzyme
-
additional information
additional information
allosterically regulated enzyme
-
additional information
additional information
allosterically regulated enzyme
-
additional information
additional information
allosterically regulated enzyme
-
additional information
additional information
-
allosterically regulated enzyme
-
additional information
additional information
steady-state kinetics of NagB in presence or absence of activators, overview
-
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105 - 220
alpha-D-glucosamine 6-phosphate
5.8 - 455
D-fructose 6-phosphate
0.044 - 1800
D-glucosamine 6-phosphate
additional information
additional information
-
105
alpha-D-glucosamine 6-phosphate
pH 8.0, 20°C, recombinant enzyme
107
alpha-D-glucosamine 6-phosphate
mutant C118Ser/C228S/C239S/D165C/S206W, at pH 7.8 and 30°C
110
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
158
alpha-D-glucosamine 6-phosphate
wild type enzyme, at pH 7.8 and 30°C
220
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
5.8
D-fructose 6-phosphate
-
pH 7.5, 30°C
44.2
D-fructose 6-phosphate
-
pH 7.3, 60°C
455
D-fructose 6-phosphate
-
pH 7.7, 30°C
0.044
D-glucosamine 6-phosphate
mutant K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
0.37
D-glucosamine 6-phosphate
-
pH 8.0, 30°C
2 - 8
D-glucosamine 6-phosphate
-
22°C, pH 8.0
2
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C
6.1
D-glucosamine 6-phosphate
mutant R172A/K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
7.8
D-glucosamine 6-phosphate
mutant K208V, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
11.4
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254F
11.8
D-glucosamine 6-phosphate
mutant R172A, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
26.7
D-glucosamine 6-phosphate
mutant W15Y/W224Y/Y254W, pH 7.5
41.2
D-glucosamine 6-phosphate
recombinant isozyme GNPDA1 268 truncation mutant, pH 8.0, 30°C, kinetic method 2
42
D-glucosamine 6-phosphate
-
per subunit, hyperbolic kinetic conditions, in presence of 1 mM N-acetylglucosamine 6-phosphate, pH 8.8
44.2
D-glucosamine 6-phosphate
recombinant isozyme GNPDA1 275 truncation mutant, pH 8.0, 30°C, kinetic method 1
61.6
D-glucosamine 6-phosphate
-
pH 8.0, 30°C, in presence of N-acetylglucosamine 6-phosphate
69.5
D-glucosamine 6-phosphate
wild-type, modified with bimane at C206, pH 7.5, 30°C
70.6
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C
70.9
D-glucosamine 6-phosphate
wild-type, modified with dansyl-aminoethyl moiety at C206, pH 7.5, 30°C
71.6
D-glucosamine 6-phosphate
wild-type, modified with bimane at C164, pH 7.5, 30°C
74
D-glucosamine 6-phosphate
recombinant isozyme GNPDA1 275 truncation mutant, pH 8.0, 30°C, kinetic method 2
75
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254F in presence of N-acetylglucosamine 6-phosphate
80
D-glucosamine 6-phosphate
mutant W15Y/F174W/W224Y, pH 7.5
96
D-glucosamine 6-phosphate
mutant C118S/C228S/C239S, pH 7.5, 30°C
97.5
D-glucosamine 6-phosphate
-
pH 7.3, 60°C
134
D-glucosamine 6-phosphate
mutant W15Y, pH 7.5
138
D-glucosamine 6-phosphate
mutant W224Y, pH 7.5
144
D-glucosamine 6-phosphate
mutant W15Y/W224Y, pH 7.5
153
D-glucosamine 6-phosphate
wild-type, pH 7.5, 30°C
158
D-glucosamine 6-phosphate
wild-type, pH 7.5
160
D-glucosamine 6-phosphate
wild-type, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate
218
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254T
228
D-glucosamine 6-phosphate
recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 1, in presence of saturating concentration of N-acetylglucosamine 6-phosphate
248
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, mutant enzyme Y254T in presence of N-acetylglucosamine 6-phosphate
255
D-glucosamine 6-phosphate
-
hexameric enzyme, hyperbolic kinetic conditions, in presence of 1 mM N-acetylglucosamine 6-phosphate, pH 8.8
260
D-glucosamine 6-phosphate
recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 2, in presence of saturating concentration of N-acetylglucosamine 6-phosphate
292
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, wild-type enzyme
320
D-glucosamine 6-phosphate
-
pH 7.7, 30°C, wild-type enzyme in presence of N-acetylglucosamine 6-phosphate
1800
D-glucosamine 6-phosphate
-
pH 7.7, 30°C
additional information
additional information
-
-
-
additional information
additional information
comparison of kcat of unmodified and N-terminal modified enzyme
-
additional information
additional information
-
comparison of kcat of unmodified and N-terminal modified enzyme
-
additional information
additional information
comparison of kcat of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
additional information
additional information
-
comparison of kcat of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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subcutaneous fat and abdominal fat, high expression level
brenda
-
-
brenda
low expression level
brenda
high expression level
brenda
low expression level
brenda
low expression level
brenda
-
brenda
high expression level
brenda
-
brenda
-
-
brenda
-
-
brenda
low expression level
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
low expression level
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
cortex
brenda
-
cortex
brenda
low expression level
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chicken
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chicken
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chicken
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chicken
brenda
additional information
-
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chicken
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chickens
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chickens
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chickens
brenda
additional information
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chickens
brenda
additional information
-
analysis of effects on the enzyme by fasting and high-glucose-fat diet treatments, association analysis of variations of GNPDA2 with productive traits in chicken tissues, overview. The complete transcript GNPDA2-a is predominantly expressed in adipose tissue (subcutaneous and abdominal fat), hypothalamus, and duodenum. In fasting chickens, the mRNA level of GNPDA2 is decreased by 58.8% in hypothalamus, and returned to normal level after refeeding. High-glucose-fat diet fed chicken show GNPDA2 gene expression about 2fold higher in adipose tissue compared to control (basal diet), but decreased expression in hypothalamus. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Tissue specific expression of GNPDA2 variants in Xinghua chicken, no significantly different in expression level of all tissues between female and male chickens
brenda
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evolution
the GNPDA2 (glucosamine-6-phosphate deaminase 2) gene is a member of glucosamine-6-phosphate (GlcN6P) deaminase subfamily
evolution
the lack of allostery as for Staphlyococcus aureus NagB has also been observed in the monomeric Staphylococcus mutans and Bacillus subtilis NagB enzymes, and supports the hypothesis that Gram-positive NagB enzymes have lost the property of allosteric regulation
evolution
-
the lack of allostery as for Staphlyococcus aureus NagB has also been observed in the monomeric Staphylococcus mutans and Bacillus subtilis NagB enzymes, and supports the hypothesis that Gram-positive NagB enzymes have lost the property of allosteric regulation
-
evolution
-
the lack of allostery as for Staphlyococcus aureus NagB has also been observed in the monomeric Staphylococcus mutans and Bacillus subtilis NagB enzymes, and supports the hypothesis that Gram-positive NagB enzymes have lost the property of allosteric regulation
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malfunction
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mutant parasites lacking GND are unable to grow in medium containing amino sugars as sole carbohydrate source and rapidly loose viability, concomitant with the hyper-accumulation of hexosamine-phosphates. Expression of native GND, but not a cytosolic form of GND, in DELTAgnd parasites restored hexosamine-dependent growth, indicating that toxicity is due to depletion of glycosomal pools of ATP. Promastigote and amastigote stages of the DELTAgnd mutant are unable to replicate within macrophages and were either completely cleared or exhibited reduced lesion development in highly susceptible Balb/c mice
malfunction
depletion of GFAT1 reduces the cellular pool of UDP-GlcNAc and hyaluronan synthesis, while simultaneous blocking of both isozymes GNPDA1 and GDPDA2 exerts opposite effects, indicating that in standard culture conditions keratinocyte GNPDAs mainly catalyze the reaction from GlcN6P back to Fru6P. When hexosamine biosynthesis is blocked by GFAT1 siRNA, the effect by GNPDAs is reversed, now catalyzing Fru6P towards GlcN6P, likely in an attempt to maintain UDPGlcNAc content. Silencing of these enzymes also changes the gene expression of related enzymes: GNPDA1 siRNA induces GFAT2 which is hardly measurable in these cells under standard culture conditions, GNPDA2 siRNA increases GFAT1, and GFAT1 siRNA increases the expression of hyaluronan synthase 2 (HAS2). Silencing of GFAT1 stimulates GNPDA1 and GDPDA2, and inhibites cell migration. The multiple delicate adjustments of these reactions demonstrate the importance of hexosamine biosynthesis in cellular homeostasis, known to be deranged in diseases like diabetes and cancer. GNPDA1 siRNA, while ineffective by itself, could largely prevent the influence of mannose on UDP-GlcNAc and hyaluronan synthesis, thus raising GNPDA1 as a specific candidate for the target of mannose. The finding that GNPDA1 siRNA does not counteract the mannose-induced depletion of cell surface hyaluronan suggests that in addition to GNPDA1 mannose may target cell surface receptor activity
malfunction
depletion of GFAT1 reduces the cellular pool of UDP-GlcNAc and hyaluronan synthesis, while simultaneous blocking of both isozymes GNPDA1 and GDPDA2 exerts opposite effects, indicating that in standard culture conditions keratinocyte GNPDAs mainly catalyze the reaction from GlcN6P back to Fru6P. When hexosamine biosynthesis is blocked by GFAT1 siRNA, the effect by GNPDAs is reversed, now catalyzing Fru6P towards GlcN6P, likely in an attempt to maintain UDPGlcNAc content. Silencing of these enzymes also changes the gene expression of related enzymes:GNPDA1 siRNA induces GFAT2 which is hardly measurable in these cells under standard culture conditions, GNPDA2 siRNA increases GFAT1, and GFAT1 siRNA increases the expression of hyaluronan synthase 2 (HAS2). Silencing of GFAT1 stimulates GNPDA1 and GDPDA2, and inhibites cell migration. The multiple delicate adjustments of these reactions demonstrate the importance of hexosamine biosynthesis in cellular homeostasis, known to be deranged in diseases like diabetes and cancer
malfunction
two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken, overview
metabolism
controlling the biosynthetic and degradative pathways of amino sugar metabolism is important in all organisms to avoid loss of nitrogen and energy via a futile cycle of synthesis and breakdown. The enzyme glucosamine-6P deaminase (NagB) is central to this control, and N-acetylglucosamine-6P is the key signaling molecule regulating amino sugar utilization in Escherichia coli
metabolism
distinct contributions of glucosamine-6-phosphate (GlcN6P):glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) and glucosamine-6-phosphate deaminases (GNPDA1 and 2) isozymes to the UDP-GlcNAc pool of cultured keratinocytes, and their consequences to the hyaluronan synthesis, one of the cellular processes most dependent on cytosolic UDP-GlcNAc supply, and to cell proliferation and migration, overview
metabolism
distinct contributions of glucosamine-6-phosphate (GlcN6P):glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) and glucosamine-6-phosphate deaminases (GNPDA1 and 2)isozymes to the UDP-GlcNAc pool of cultured keratinocytes, and their consequences to the hyaluronan synthesis, one of the cellular processes most dependent on cytosolic UDP-GlcNAc supply, and to cell proliferation and migration, overview
metabolism
NanE, GlcNAc-6P epimerase, and the uridylylated PII protein allosterically activate NagB by direct protein-protein interactions. NanE is essential for N-acetylneuraminic acid (NANA) and N-acetylmannosamine (ManNAc) utilization, and the PII protein is known to be a central metabolic nitrogen regulator. Regulatory links between carbon and nitrogen metabolism are important for adaptation of metabolism to different growth conditions. Regulatory interdependence between different metabolic pathways
physiological function
hGNPDA1 can be important for the maintenance of an adequate level of the pool of the UDP-GlcNAc6P, the N-acetylglucosylaminyl donor for many reactions in the cell
physiological function
NagB, a glucosamine 6-phosphate deaminase in Escherichia coli, is essential for amino sugar utilization and is known to be allosterically regulated by N-acetylglucosamine 6-phosphate (GlcNAc-6P) and the histidine-phosphorylatable phosphocarrier protein, HPr. Specific physiological functions for the regulation of NagB by its three protein activators
physiological function
the enzyme glucosamine-6P deaminase (NagB) is required for growth on both GlcN and GlcNAc. It is an allosteric enzyme in Escherichia coli, displaying sigmoid kinetics with respect to its substrate, GlcN6P, and is allosterically activated by GlcNAc6P. The high concentration of GlcN6P, accompanied by the small increase in GlcNAc6P, drives Escherichia coli NagB (NagBEc) into its high activity state, as observed during growth on GlcN
physiological function
the GNPDA2 gene encodes an allosteric enzyme of glucosamine 6-phosphate deaminase (GlcN6P), which can catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose-6-phosphate and ammonium. The GNPDA2 gene has a potential role in the regulation of body weight, fat and energy metabolism in chicken
additional information
possible functional significance of the C-terminal extension of hGNPDA1 isozyme, which is not present in isoform 2
additional information
possible functional significance of the C-terminal extension of hGNPDA1 isozyme, which is not present in isoform 2
additional information
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possible functional significance of the C-terminal extension of hGNPDA1 isozyme, which is not present in isoform 2
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C118S/C228S/C239S
decrease in kcat-value, no modification of allosteric activation
C118Ser/C228S/C239S/D165C/S206W
the mutant shows reduced turnover number compared to the wild type enzyme
C219S
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the kinetic and allosteric properties of the mutant enzyme in which Ser replaces Cys219 or Cys228 are the same as those described for the wild-type enzyme. The same result is obtained with the double mutation
C228S
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the kinetic and allosteric properties of the mutant enzyme in which Ser replaces Cys219 or Cys228 are the same as those described for the wild-type enzyme. The same result is obtained with the double mutation
D141N
the mutation modifies the kcat versus pH profile of the enzyme
D141N/E148Q
mutation modifies the kcat versus pH profile of the enzyme
E148Q
the mutation modifies the kcat versus pH profile of the enzyme
H143Q
drastically impairs the activity of the enzyme in the forward but not in the backward direction of the reaction
K208E
entirely inactive in absence of allosteric activator N-acetylglucose-6-phosphate
K208V
homotropic cooperativity, Hill-coefficient 1.7, 2fold increase in dissociation constant for allosteric activator N-acetylglucose-6-phosphate compared to wild-type
R172A
inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant
R172A/K208E
inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant
W15Y
mutant containing a single Trp residue at W224
W15Y/F174W/W224Y
mutant containing a single, new Trp-residue at F174W
W15Y/W224Y
mutant without Trp residues
W15Y/W224Y/Y254W
mutant containing a single, new Trp-residue at Y254W
W224Y
mutant containing a single Trp residue at W15
Y121T
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while the wild-type enzyme behaves as a classical allosteric K-system which can be described by the allosteric concerted model, the mutant forms Y121T and Y121W present an asymmetric behaviour towards the allosteric activator, which can be described as two distinct half-of-the-sites allosteric activation steps occuring with different affinities for the N-acetyl-D-glucosamine 6-phosphate
Y121W
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while the wild-type enzyme behaves as a classical allosteric K-system which can be described by the allosteric concerted model, the mutant forms Y121T and Y121W present an asymmetric behaviour towards the allosteric activator, which can be described as two distinct half-of-the-sites allosteric activation steps occuring with different affinities for the N-acetyl-D-glucosamine 6-phosphate
Y254F
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the mutant is less active than wild-type enzyme, the replacement causes an uncoupling of the homotropic and heterotrophic effects
Y254T
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the mutation results in pure K-system with a similar catalytic activity to that of the wild-type enzyme, mutant displays kcat values similar to the wild-type enzyme
F174A
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the mutation effectively weakens the interaction between the active-site lid and the rest of the enzyme molecule, the mutant is essentially inactive in the absence of its allosteric activator
F174A
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the mutant requires higher concentrations of N-acetylglucosamine-6-phosphate for activity in vitro. The mutant strain grows better on glucosamine in the presence of N-acetylglucosamine-6-phosphate
additional information
recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, no effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB
additional information
-
recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, no effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB
additional information
-
recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, no effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB
-
additional information
construction of bacterial strains LAA199 (nagBEc+) and LAA195 (nagBBs+). The gene for the Escherichia coli allosteric NagBEc enzyme is replaced with that of the nonallosteric Bacillus subtilis homologue NagBBs. No effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB. Deletion of the nagB gene had no strong effect on the amino sugar pools
additional information
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construction of bacterial strains LAA199 (nagBEc+) and LAA195 (nagBBs+). The gene for the Escherichia coli allosteric NagBEc enzyme is replaced with that of the nonallosteric Bacillus subtilis homologue NagBBs. No effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB. Deletion of the nagB gene had no strong effect on the amino sugar pools
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotyped results of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotyped results of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotyped results of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotyped results of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
-
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotyped results of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotypes resulting of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotypes resulting of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotypes resulting of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotypes resulting of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
-
enzyme GNPDA2 overexpression and small interfering RNA (siRNA) knockout in chicken preadipocytes, phenotypes, overview. Two single-nucleotide polymorphisms of the GNPDA2 gene are significantly associated with body weight and a number of fatness traits in chicken. Two SNPs, g.6667C > T and g.7393C > T, in 3'-UTR are significantly associated with a number of productive traits in chicken. The genotypes resulting of these two SNPs are also confirmed by PCR-RFLP. The g.6667C > T and g.7393C > T (rs14486239) are both significantly associated with body weight during early stage (1-28 days old) of growth. The g.6667C > T is also significantly associated with chest depth and abdominal fat pad weight. The g.7393C > T is significantly associated with small intestine length, leg muscle weight, dressed weight, eviscerated weight, and semi-eviscerated weight
additional information
generation of mutants truncated at positions 260 and 275
additional information
generation of mutants truncated at positions 260 and 275
additional information
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generation of mutants truncated at positions 260 and 275
additional information
siRNA silencing of isozymes GNPDA1 and GDPDA2 with or withour simultanious silencing of glucosamine-6-phosphate (GlcN6P): glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) isozymes, phenotypes, overview. Analysis of influences of the siRNAs against genes regulating hexosamine biosynthesis on mRNA levels of GFAT1, GNPDA1, and GNPDA2 by quantitative RT-PCR expression analysis. Cell proliferation and migration following GFAT and GNPDA depletion
additional information
siRNA silencing of isozymes GNPDA1 and GDPDA2 with or withour simultanious silencing of glucosamine-6-phosphate (GlcN6P): glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) isozymes, phenotypes, overview. Analysis of influences of the siRNAs against genes regulating hexosamine biosynthesis on mRNA levels of GFAT1, GNPDA1, and GNPDA2 by quantitative RT-PCR expression analysis. Cell proliferation and migration following GFAT and GNPDA depletion
additional information
-
siRNA silencing of isozymes GNPDA1 and GDPDA2 with or withour simultanious silencing of glucosamine-6-phosphate (GlcN6P): glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) isozymes, phenotypes, overview. Analysis of influences of the siRNAs against genes regulating hexosamine biosynthesis on mRNA levels of GFAT1, GNPDA1, and GNPDA2 by quantitative RT-PCR expression analysis. Cell proliferation and migration following GFAT and GNPDA depletion
additional information
siRNA silencing of isozymes GNPDA1 and GDPDA2 with or without simultanious silencing of glucosamine-6-phosphate (GlcN6P):glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) isozymes, phenotypes, overview. Analysis of influences of the siRNAs against genes regulating hexosamine biosynthesis on mRNA levels of GFAT1, GNPDA1, and GNPDA2 by quantitative RT-PCR expression analysis. Cell proliferation and migration following GFAT and GNPDA depletion. GNPDA1 siRNA, while ineffective by itself, can largely prevent the influence of mannose on UDP-GlcNAc and hyaluronan synthesis, thus raising GNPDA1 as a specific candidate for the target of mannose. The finding that GNPDA1 siRNA does not counteract the mannose-induced depletion of cell surface hyaluronan suggests that in addition to GNPDA1 mannose may target cell surface receptor activity
additional information
siRNA silencing of isozymes GNPDA1 and GDPDA2 with or without simultanious silencing of glucosamine-6-phosphate (GlcN6P):glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) isozymes, phenotypes, overview. Analysis of influences of the siRNAs against genes regulating hexosamine biosynthesis on mRNA levels of GFAT1, GNPDA1, and GNPDA2 by quantitative RT-PCR expression analysis. Cell proliferation and migration following GFAT and GNPDA depletion. GNPDA1 siRNA, while ineffective by itself, can largely prevent the influence of mannose on UDP-GlcNAc and hyaluronan synthesis, thus raising GNPDA1 as a specific candidate for the target of mannose. The finding that GNPDA1 siRNA does not counteract the mannose-induced depletion of cell surface hyaluronan suggests that in addition to GNPDA1 mannose may target cell surface receptor activity
additional information
-
siRNA silencing of isozymes GNPDA1 and GDPDA2 with or without simultanious silencing of glucosamine-6-phosphate (GlcN6P):glutamine-fructose-6-phosphate aminotransferases (GFAT1 and 2) isozymes, phenotypes, overview. Analysis of influences of the siRNAs against genes regulating hexosamine biosynthesis on mRNA levels of GFAT1, GNPDA1, and GNPDA2 by quantitative RT-PCR expression analysis. Cell proliferation and migration following GFAT and GNPDA depletion. GNPDA1 siRNA, while ineffective by itself, can largely prevent the influence of mannose on UDP-GlcNAc and hyaluronan synthesis, thus raising GNPDA1 as a specific candidate for the target of mannose. The finding that GNPDA1 siRNA does not counteract the mannose-induced depletion of cell surface hyaluronan suggests that in addition to GNPDA1 mannose may target cell surface receptor activity
additional information
-
generation of enzyme-deficient DELTAgnd mutants, phenotype, detailed overview
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Comb, D.G.; Roseman, S.
Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase
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Purification of glucosamine 6-phosphate deaminase from human brain
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Studies on the mechanism of Escherichia coli glucosamine-6-phosphate isomerase
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Glucosamine metabolism in Drosophila salivary glands. Separation of metabolites and some characteristics of three enzymes involved
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Purification and some properties of inducible glucosamine-6-phosphate deaminase from Candida albicans
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Glucosamine 6-P isomerase of Erwinia prunastri (L.) Ach.
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Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from Escherichia coli
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Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli
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Purification and characterization of encystment-induced glucosamine 6-phosphate isomerase in Giardia
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Oliva, G.; Fontes, M.R.; Garratt, R.C.; Altamirano, M.M.; Calcagno, M.L.; Horjales, E.
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution
Structure
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Escherichia coli
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Altamirano, M.M.; Plumbridge, J.A.; Barba, H.A.; Calcagno, M.L.
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Asymmetric allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase produced by replacement of Tyr121
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