Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein.
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Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenaseStructure of the proline dehydrogenase domain of the multifunctional PutA flavoproteinRedox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡Structural Basis of the Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutACrystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicumProline utilization by Bacillus subtilis: uptake and catabolismDivergent structure and regulatory mechanism of proline catabolic systems: characterization of the putAP proline catabolic operon of Pseudomonas aeruginosa PAO1 and its regulation by PruR, an AraC/XylS family proteinGenomic sequence of Spodoptera frugiperda Ascovirus 1a, an enveloped, double-stranded DNA insect virus that manipulates apoptosis for viral reproductionFlavin redox switching of protein functionsProline catabolism by Pseudomonas putida: cloning, characterization, and expression of the put genes in the presence of root exudates.Network analysis of the transcriptional pattern of young and old cells of Escherichia coli during lag phase.The arthrobacter arilaitensis Re117 genome sequence reveals its genetic adaptation to the surface of cheese.Complete genome sequence of Corynebacterium variabile DSM 44702 isolated from the surface of smear-ripened cheeses and insights into cheese ripening and flavor generationCharacterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor.Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzymeRegulation of PutA-membrane associations by flavin adenine dinucleotide reductionΔ(1)-pyrroline-5-carboxylate/glutamate biogenesis is required for fungal virulence and sporulation.Isolation, DNA sequence analysis, and mutagenesis of a proline dehydrogenase gene (putA) from Bradyrhizobium japonicumRelationships within the aldehyde dehydrogenase extended family.Unique structural features and sequence motifs of proline utilization A (PutA).Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli.Proline mechanisms of stress survival.Environmental and developmental signals modulate proline homeostasis: evidence for a negative transcriptional regulator.Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).The completely sequenced plasmid pEST4011 contains a novel IncP1 backbone and a catabolic transposon harboring tfd genes for 2,4-dichlorophenoxyacetic acid degradation.Control of expression of divergent Pseudomonas putida put promoters for proline catabolismThe Agaricus bisporus pruA gene encodes a cytosolic delta 1-pyrroline-5-carboxylate dehydrogenase which is expressed in fruit bodies but not in gill tissue.Expression of the putA gene encoding proline dehydrogenase from Rhodobacter capsulatus is independent of NtrC regulation but requires an Lrp-like activator proteinFunctional versatility and molecular diversity of the metabolic map of Escherichia coli.Microbial production of N-acetyl cis-4-hydroxy-L-proline by coexpression of the Rhizobium L-proline cis-4-hydroxylase and the yeast N-acetyltransferase Mpr1.A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis.The benzodiazepine-like natural product tilivalline is produced by the entomopathogenic bacterium Xenorhabdus eapokensis.Physiological Response of to Increasingly Nutrient-Rich Growth Conditions
P2860
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P2860
Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@en
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@nl
type
label
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@en
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@nl
prefLabel
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@en
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@nl
P2093
P356
P1476
Sequence analysis identifies t ...... Escherichia coli PutA protein.
@en
P2093
P304
P356
10.1006/JMBI.1994.1696
P407
P577
1994-11-01T00:00:00Z