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GDP-2-azido-2-deoxy-D-glucose + Glcbeta1,3-GalNAc-PP-CPh
?
GDP-2-azido-2-deoxy-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
?
GDP-4-azido-4-deoxy-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
?
GDP-D-glucopyranosylamine + Glcbeta1,3-GalNAc-PP-CPh
?
-
67% activity compared to GDP-D-mannose
-
-
?
GDP-D-glucose + Glcbeta1,3-GalNAc-PP-CPh
?
-
66% activity compared to GDP-D-mannose
-
-
?
GDP-D-mannobiosyl fluoride + Glcbeta1,3-GalNAc-PP-CPh
?
-
88% activity compared to GDP-D-mannose
-
-
?
GDP-D-mannopyranosylamine + Glcbeta1,3-GalNAc-PP-CPh
?
-
64% activity compared to GDP-D-mannose
-
-
?
GDP-D-mannose + Glcbeta1,3-GalNAc-PEG
Man-alpha1-P-6-Glc-beta1,3-GalNAc-PEG + GMP
-
-
-
-
?
GDP-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
Man-alpha1-P-6-Glc-beta1,3-GalNAc-PP-CPh + GMP
-
100% activity
-
-
?
GDP-D-talose + Glcbeta1,3-GalNAc-PP-CPh
?
-
48% activity compared to GDP-D-mannose
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose [side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose[side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxyglucose[side 1]
[protein]-L-histidine + 2-deoxyglucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucosaminate[side 1]
[protein]-L-histidine + D-glucosaminate 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine [side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side 2]
additional information
?
-
GDP-2-azido-2-deoxy-D-glucose + Glcbeta1,3-GalNAc-PP-CPh
?
-
61% activity compared to GDP-D-mannose
-
-
?
GDP-2-azido-2-deoxy-D-glucose + Glcbeta1,3-GalNAc-PP-CPh
?
-
61% activity compared to GDP-D-mannose
-
-
?
GDP-2-azido-2-deoxy-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
?
-
86% activity compared to GDP-D-mannose
-
-
?
GDP-2-azido-2-deoxy-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
?
-
86% activity compared to GDP-D-mannose
-
-
?
GDP-4-azido-4-deoxy-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
?
-
31% activity compared to GDP-D-mannose
-
-
?
GDP-4-azido-4-deoxy-D-mannose + Glcbeta1,3-GalNAc-PP-CPh
?
-
31% activity compared to GDP-D-mannose
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose [side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose [side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxyglucose[side 1]
[protein]-L-histidine + 2-deoxyglucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + 2-deoxyglucose[side 1]
[protein]-L-histidine + 2-deoxyglucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine [side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + N-acetyl-D-glucosamine [side 1]
[protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side 2]
-
-
-
-
?
additional information
?
-
-
the enzyme possesses a strict acceptor specificity toward Glc-beta1,3-GalNAc-diphospho-lipids
-
-
-
additional information
?
-
-
the enzyme shows no activity with GDP-Glc2dO, GDP-L-fucose, GDP-L-galactose, GTP, UDP-D-mannose, UDP-D-glucose, and CMPNeu5Ac
-
-
-
additional information
?
-
-
the enzyme possesses a strict acceptor specificity toward Glc-beta1,3-GalNAc-diphospho-lipids
-
-
-
additional information
?
-
-
the enzyme shows no activity with GDP-Glc2dO, GDP-L-fucose, GDP-L-galactose, GTP, UDP-D-mannose, UDP-D-glucose, and CMPNeu5Ac
-
-
-
additional information
?
-
-
the enzyme is the major transporter for D-mannose and also transports efficiently D-glucose, 2-deoxyglucose, D-fructose, N-acetylglucosamine, and glucosamine
-
-
?
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[protein]-Npi-phospho-L-histidine + 2-deoxy-D-glucose[side 1]
[protein]-L-histidine + 2-deoxy-D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-fructose[side 1]
[protein]-L-histidine + D-fructose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucosaminate[side 1]
[protein]-L-histidine + D-glucosaminate 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-glucose[side 1]
[protein]-L-histidine + D-glucose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
additional information
?
-
-
the enzyme is the major transporter for D-mannose and also transports efficiently D-glucose, 2-deoxyglucose, D-fructose, N-acetylglucosamine, and glucosamine
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
[protein]-Npi-phospho-L-histidine + D-mannose[side 1]
[protein]-L-histidine + D-mannose 6-phosphate[side 2]
-
-
-
-
?
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Acute Lung Injury
Hypoxia induces expression of angiotensin-converting enzyme II in alveolar epithelial cells: Implications for the pathogenesis of acute lung injury in COVID-19.
Atrial Fibrillation
Relation between angiotensin-converting enzyme II genotype and atrial fibrillation in Japanese patients with hypertrophic cardiomyopathy.
Cardiomyopathy, Hypertrophic
Relation between angiotensin-converting enzyme II genotype and atrial fibrillation in Japanese patients with hypertrophic cardiomyopathy.
Coronavirus Infections
Single-cell analysis of angiotensin-converting enzyme II expression in human kidneys and bladders reveals a potential route of 2019 novel coronavirus infection.
COVID-19
Angiotensin-converting enzyme II expression and its implication in the association between COVID-19 and allergic rhinitis.
COVID-19
Biophysical analysis of SARS-CoV-2 transmission and theranostic development via N protein computational characterization.
COVID-19
Coronavirus disease-19 and the gut-lung axis.
COVID-19
Down-Regulation of Colonic ACE2 Expression in Patients With Inflammatory Bowel Disease Responding to Anti-TNF Therapy: Implications for COVID-19.
COVID-19
Hypoxia induces expression of angiotensin-converting enzyme II in alveolar epithelial cells: Implications for the pathogenesis of acute lung injury in COVID-19.
COVID-19
Oroxylin A is a severe acute respiratory syndrome coronavirus 2-spiked pseudotyped virus blocker obtained from Radix Scutellariae using angiotensin-converting enzyme II/cell membrane chromatography.
COVID-19
Pharmacological perspective: glycyrrhizin may be an efficacious therapeutic agent for COVID-19.
COVID-19
Role of Oxidative Stress on SARS-CoV (SARS) and SARS-CoV-2 (COVID-19) Infection: A Review.
COVID-19
Single-cell analysis of angiotensin-converting enzyme II expression in human kidneys and bladders reveals a potential route of 2019 novel coronavirus infection.
COVID-19
The war against the SARS-CoV2 infection: Is it better to fight or mitigate it?
COVID-19
Traditional Chinese medicine network pharmacology study on exploring the mechanism of Xuebijing Injection in the treatment of coronavirus disease 2019.
COVID-19
Wildland firefighter exposure to smoke and COVID-19: A new risk on the fire line.
Dental Caries
Coordinated Regulation of the EII(Man) and fruRKI Operons of Streptococcus mutans by Global and Fructose-Specific Pathways.
Endocarditis
Genome-wide screening identifies PTS permease BepA to be involved in Enterococcus faecium endocarditis and biofilm formation.
Heart Failure
Bioanalytical Assessment of Plasma Concentrations of Angiotensin-Converting Enzyme II Inhibitors and Angiotensin Receptor Blockers: A Pilot Study Among Patients Hospitalized With Acute Heart Failure.
Heart Failure
Increased expression of the renin-angiotensin system and mast cell density but not of angiotensin-converting enzyme II in late stages of human heart failure.
Hemorrhagic Stroke
COVID-19 Associated Ischemic Stroke and Hemorrhagic Stroke: Incidence, Potential Pathological Mechanism, and Management.
Hypertension, Pulmonary
The beneficial effects of angiotensin-converting enzyme II (ACE2) activator in pulmonary hypertension secondary to left ventricular dysfunction.
Infections
Engineered ACE2 receptor traps potently neutralize SARS-CoV-2.
Infections
Exploring the Mystery of Angiotensin-Converting Enzyme II (ACE2) in the Battle against SARS-CoV-2.
Infections
Facilitation of bacteriophage lambda DNA injection by inner membrane proteins of the bacterial phosphoenol-pyruvate: carbohydrate phosphotransferase system (PTS).
Infections
Regulation Mechanism for the Binding between the SARS-CoV-2 Spike Protein and Host Angiotensin-Converting Enzyme II.
Infections
Role of Oxidative Stress on SARS-CoV (SARS) and SARS-CoV-2 (COVID-19) Infection: A Review.
Infections
The levanase operon of Bacillus subtilis expressed in Escherichia coli can substitute for the mannose permease in mannose uptake and bacteriophage lambda infection.
Infections
Two subunits of mannose permease, II-PMan and II-MMan, of Escherichia coli mediate coliphage N4 infection.
Intellectual Disability
A family-based association study of DIO2 and children mental retardation in the Qinba region of China.
Lung Injury
Identification of potent human neutralizing antibodies against SARS-CoV-2 implications for development of therapeutics and prophylactics.
Lung Neoplasms
Distinct effects of asthma and COPD comorbidity on disease expression and outcome in patients with COVID-19.
Neoplasms
Sequence analysis of a 45-kb segment in the 19 degrees-23 degrees region of the Bacillus subtilis chromosome containing glpT and mpr loci.
Neoplasms
Solubilized nuclear DNA-dependent RNA polymerases from normal rat mammary glands and from transplantable R-35 rat mammary tumors.
Paraganglioma
Chromosome 11 monosomy in conjunction with a mutated SDHD initiation codon in nonfamilial paraganglioma cases.
Pneumonia, Viral
Biophysical analysis of SARS-CoV-2 transmission and theranostic development via N protein computational characterization.
Rhinitis, Allergic
Angiotensin-converting enzyme II expression and its implication in the association between COVID-19 and allergic rhinitis.
Severe Acute Respiratory Syndrome
A Fatal Extrapulmonary Manifestation of COVID-19.
Severe Acute Respiratory Syndrome
Combating sars-cov-2 through lipoxins, proteasome, caveolin and nuclear factor-?b pathways in non-pregnant and pregnant populations.
Severe Acute Respiratory Syndrome
Coronavirus Disease 2019 and Nasal Conditions: A Review of Current Evidence.
Severe Acute Respiratory Syndrome
Coronavirus Disease 2019: Clinical Review.
Severe Acute Respiratory Syndrome
Effect of COVID-19 on Male Reproductive System - A Systematic Review.
Severe Acute Respiratory Syndrome
Engineered ACE2 receptor traps potently neutralize SARS-CoV-2.
Severe Acute Respiratory Syndrome
Interactions between antihyperglycemic drugs and the renin-angiotensin system: Putative roles in COVID-19. A mini-review.
Severe Acute Respiratory Syndrome
Oroxylin A is a severe acute respiratory syndrome coronavirus 2-spiked pseudotyped virus blocker obtained from Radix Scutellariae using angiotensin-converting enzyme II/cell membrane chromatography.
Severe Acute Respiratory Syndrome
Regulation Mechanism for the Binding between the SARS-CoV-2 Spike Protein and Host Angiotensin-Converting Enzyme II.
Severe Acute Respiratory Syndrome
Single-cell analysis of angiotensin-converting enzyme II expression in human kidneys and bladders reveals a potential route of 2019 novel coronavirus infection.
Ventricular Dysfunction, Left
The beneficial effects of angiotensin-converting enzyme II (ACE2) activator in pulmonary hypertension secondary to left ventricular dysfunction.
Virus Diseases
Biophysical analysis of SARS-CoV-2 transmission and theranostic development via N protein computational characterization.
Virus Diseases
Coronavirus Disease 2019 and Nasal Conditions: A Review of Current Evidence.
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malfunction
-
a 2-deoxyglucose-induced selective defect in the membrane component ElI man of the phosphoenolpyruvate:mannose phosphotransferase system can partially release glucose-mediated catabolite repression but not fructose-mediated catabolite repression in soy pediococci
malfunction
-
a 2-deoxyglucose-induced selective defect in the membrane component ElI man of the phosphoenolpyruvate:mannose phosphotransferase system can partially release glucose-mediated catabolite repression but not fructose-mediated catabolite repression in soy pediococci
-
metabolism
-
small RNA SgrS-mediated down regulation of the enzyme is required for growth rescue in the presence of 2-deoxyglucose
metabolism
-
the enzyme is also required for utilization of D-glucosaminate
metabolism
-
the enzyme is an important component in catabolite repression in Lactobacillus pentosus and regulates the synthesis of the enzyme EIIFru
metabolism
-
the gene products of genes manX, man Y and manZ are involved in mannose uptake. In addition, man Y codes for the Pel function, necessary for penetration of lambda-DNA
metabolism
-
Man-PTS subunits IIC and IID are necessary for bacteriocin BacSJ activity
metabolism
-
the enzyme is responsible for the formation of the Man-alpha1-P-6-Glc linkage in Clostridium difficile polysaccharide II
metabolism
-
the enzyme is the dominant transporter for glucose, mannose, galactose, glucosamine and N-acetylglucosamine, and has a dominant influence on sugar-specific, CcpA-independent catabolite repression
metabolism
-
the enzyme is an important component in catabolite repression in Lactobacillus pentosus and regulates the synthesis of the enzyme EIIFru
-
metabolism
-
Man-PTS subunits IIC and IID are necessary for bacteriocin BacSJ activity
-
metabolism
-
the enzyme is responsible for the formation of the Man-alpha1-P-6-Glc linkage in Clostridium difficile polysaccharide II
-
metabolism
-
the enzyme is the dominant transporter for glucose, mannose, galactose, glucosamine and N-acetylglucosamine, and has a dominant influence on sugar-specific, CcpA-independent catabolite repression
-
physiological function
-
all three subunits. IIIMan, II-PMm and II-MMan are required for sugar transport and phosphorylation, while subunits II-PMm and II-MMan alone are sufficient for penetration of lambda DNA
physiological function
-
EIItMantexpression leads to an enhanced sensitivity of Enterococcus faecalis to the bacteriocin mesentericin Y105
physiological function
mannose-specific phosphotransferase system component IID represses expression of suilysin in serotype 2 Streptococcus suis
physiological function
-
the enzyme and especially subunit MptD is involved in sensitivity to mesentericin Y105
physiological function
-
the enzyme is required for mannose transport and penetration of lambdaDNA in Escherichia coli K-12
physiological function
-
the enzyme participates in glucose-mediated carbon catabolite repression and downregulation of virulence gene expression, and it is the receptor for class IIa bacteriocins
physiological function
-
both IIC and IID components of the mannose phosphotransferase system play an important role in the specific recognition between the bacteriocin-receptor complex and the immunity protein PedB. PedB directly interacts with the IIC protein, IID protein and pediocin PA-1 to form a complex, therefore preventing membrane permeabilization and cell death
physiological function
-
mannose-specific phosphotransferase system component IID represses expression of suilysin in serotype 2 Streptococcus suis
-
physiological function
-
both IIC and IID components of the mannose phosphotransferase system play an important role in the specific recognition between the bacteriocin-receptor complex and the immunity protein PedB. PedB directly interacts with the IIC protein, IID protein and pediocin PA-1 to form a complex, therefore preventing membrane permeabilization and cell death
-
physiological function
-
the enzyme and especially subunit MptD is involved in sensitivity to mesentericin Y105
-
physiological function
-
the enzyme participates in glucose-mediated carbon catabolite repression and downregulation of virulence gene expression, and it is the receptor for class IIa bacteriocins
-
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Aboulwafa, M.; Saier, M.H., Jr.
Soluble sugar permeases of the phosphotransferase system in Escherichia coli: Evidence for two physically distinct forms of the proteins in vivo
Mol. Microbiol.
48
131-141
2003
Escherichia coli, Escherichia coli 301
brenda
Miller, K.A.; Phillips, R.S.; Mrazek, J.; Hoover, T.R.
Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes
J. Bacteriol.
195
4057-4066
2013
Salmonella enterica
brenda
Vu-Khac, H.; Miller, K.W.
Regulation of mannose phosphotransferase system permease and virulence gene expression in Listeria monocytogenes by the EII(t)Man transporter
Appl. Environ. Microbiol.
75
6671-6678
2009
Listeria monocytogenes, Listeria monocytogenes BAA-679
brenda
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