PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM.
about
Sequence homologies between proteins of bacterial phosphoenolpyruvate-dependent sugar phosphotransferase systems: identification of possible phosphate-carrying histidine residuesPyrophosphate:protein phosphotransferase: a membrane-bound enzyme of endoplasmic reticulumCatabolite-insensitive revertants of lac promoter mutantsPhosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteriaPurification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-alpha-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyzes maltose 6-phosphate and related phospho-alpha-D-glucosidesPyruvate kinase: Function, regulation and role in cancerRegulating the Intersection of Metabolism and Pathogenesis in Gram-positive BacteriaThe involvement of transport proteins in transcriptional and metabolic regulationPhosphotransferase-dependent accumulation of (p)ppGpp in response to glutamine deprivation in Caulobacter crescentus.The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-pSolution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase systemSolution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase systemSolution structure of the phosphoryl transfer complex between the signal-transducing protein IIAGlucose and the cytoplasmic domain of the glucose transporter IICBGlucose of the Escherichia coli glucose phosphotransferase systemSolution Structure of the IIAChitobiose-IIBChitobiose Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemCrystal structure of a phosphorylation-coupled saccharide transporterStructural Insights into the Substrate Specificity of a 6-Phospho- -glucosidase BglA-2 from Streptococcus pneumoniae TIGR4Solution Structure of the IIAChitobiose-HPr Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemMemoirs of a biochemical hod carrierThe dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor.Isolation of a glucosamine-specific kinase, a unique enzyme of Vibrio choleraeEfflux and the steady state in alpha-methylglucoside transport in Escherichia coli.Compartmentation in the induction of the hexose-6-phosphate transport system of Escherichia coliNew protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression.Unraveling the evolutionary history of the phosphoryl-transfer chain of the phosphoenolpyruvate:phosphotransferase system through phylogenetic analyses and genome context.Expression of the human erythrocyte glucose transporter in Escherichia coliThe role of phosphatidylglycerol in the vectorial phosphorylation of sugar by isolated bacterial membrane preparations.A density label for membranes.The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Carbohydrate accumulation and metabolism in Escherichia coli: the close linkage and chromosomal location of ctr mutations.Distribution of the phosphoenolpyruvate: glucose phosphotransferase system in bacteria.Role of metabolic energy in the transport of -galactosides by Streptococcus lactisBeta-D-phosphogalactoside galactohydrolase from Streptococcus cremoris HP: purification and enzyme propertiesPhosphoenolpyruvate-dependent formation of D-fructose 1-phosphate by a four-component phosphotransferase system.Beta-glucoside permeases and phospho beta-glucosidases in Aerobacter aerogenes: relationship with cryptic phospho beta-glucosidases in EnterobacteriaceaeThe HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding.Expression, purification, crystallization and preliminary X-ray analysis of the EIICGlc domain of the Escherichia coli glucose transporterFluorescence changes of a membrane-bound dye during bacteriophage T5 infection of Escherichia coliGenetic control of manno(fructo)kinase activity in Escherichia coli.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Cyclic adenosine 5'-monophosphate in Escherichia coli.
P2860
Q24605280-5891DBA7-9AFB-4A87-9BC7-6CBF85ED1C29Q24620762-A48F2448-E93B-44E8-AFE2-417D494E3F41Q24634214-68610782-821F-4190-BA17-89B5BFF78B30Q24634652-D81A7C9E-AB58-433F-B61D-B7DD7B3407F4Q24673507-CD285ADB-ED12-4256-BB86-93E019003173Q26798084-6147AB34-10B4-46BE-A06D-18E9FDE595ACQ26799806-ED25D9F6-42AC-4114-A6CF-B6F7C7C56FA3Q26849560-F180F566-CB31-4069-BA28-A99D83F6F71BQ27318553-3A3DE078-F834-496D-8995-A74DCDE42CD3Q27619116-6A0C03C0-E351-4A75-8BCB-0205FFEB5498Q27627801-9246FBF5-E6BA-4CAF-A656-DC85A939CF95Q27639553-8EF95437-A1F1-4307-A903-DE6CE367791CQ27641064-8141C5EE-6AB8-48BF-AAF6-ECF0635C7622Q27658430-05908B9E-EE50-4AB1-A53F-4B6E314B5BB3Q27667450-11CA79A5-3241-4FA2-9EC4-E4EB032A80AEQ27677335-DBDDD6A2-E52E-47BA-9A0D-26E6731541CEQ27679135-C262F043-922F-4BF4-A0D1-5DD38F8172BBQ28205950-D4D6F313-3965-47A8-B3E9-481B0B701702Q28364958-3EE72681-2DCF-4C45-9BEF-0E529AD90C0DQ28485733-60BA2E13-70E2-4449-B66C-EF9D26BCA834Q30451487-AC534165-0DB1-48B9-A217-300F6303AC65Q30451506-8E279360-5689-4EA2-B17A-B7E62737E2CBQ32123411-08E0421C-DFC2-48D6-AF21-396DCCA68D10Q33335317-14267BFD-88C8-4DDE-94E4-804FDE8C8FEDQ33634974-02A6541F-7F46-473B-AAAA-53502F711476Q33692462-7D51C539-1B1C-4B5E-BB70-C2A7C9E6D4FFQ33704939-C7B4EF21-2A1A-4E0C-8391-65C5C3C2DECEQ33743505-D1451DCE-80A4-47BC-B4C9-103F4DFEC8C7Q33765831-B6326E58-BA55-47CB-AEC6-040B9508324FQ33773683-B06625C0-1C58-4D6F-BE52-4918804A6001Q33779125-2A4601A8-2BE9-4309-8608-0773C365E19BQ33793272-41924957-3C0C-4ED8-A793-8C2D6CE30269Q33809109-4511A694-A7C5-4EBE-B885-2ADEA350F0CEQ33813302-8F4DC5B0-E65B-4FD7-A8EB-B2C448117929Q33886626-FBDA01C4-B2E6-46A4-BFBB-BA61CFC79A14Q33902140-7C3228B5-2503-4E20-BED9-B0BC53B73099Q33913486-3C5F248B-7DA0-437C-9098-56EF2CDFFE86Q33953095-C09B75AE-510E-4948-8D85-2819C7F26A95Q34038287-4005900D-BF7D-4C36-92EC-4700C3FF2314Q34071953-784F6383-122D-4FA0-AC73-D44FDAF22F7F
P2860
PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM.
description
1964 nî lūn-bûn
@nan
1964 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1964 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1964年の論文
@ja
1964年論文
@yue
1964年論文
@zh-hant
1964年論文
@zh-hk
1964年論文
@zh-mo
1964年論文
@zh-tw
1964年论文
@wuu
name
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@ast
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@en
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@nl
type
label
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@ast
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@en
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@nl
prefLabel
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@ast
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@en
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@nl
P2093
P2860
P356
P1476
PHOSPHATE BOUND TO HISTIDINE I ...... EL PHOSPHO-TRANSFERASE SYSTEM.
@en
P2093
P2860
P304
P356
10.1073/PNAS.52.4.1067
P407
P577
1964-10-01T00:00:00Z