Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Pseudomonas jessenii

ABSTRACT: Pseudomonas jessenii overview

PROVIDER: PRJNA396613 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other
	SRR4176930_subreads.fastq.gz	Fastqsanger.gz
	SRR4176928_subreads.fastq.gz	Fastqsanger.gz
	SRR4176929_subreads.fastq.gz	Fastqsanger.gz
	SRR7168458_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 6

Similar Datasets

Pseudomonas jessenii strain:E2333

Project description:Pseudomonas jessenii E2333 genome sequencing

| PRJNA456364 | ENA

Pseudomonas jessenii strain:HY72

Project description:Pseudomonas jessenii strain:HY72 Genome sequencing

| PRJNA1184010 | ENA

Pseudomonas jessenii QYQ-1

Project description:Pseudomonas jessenii QYQ-1 Raw sequence reads

| PRJNA1087297 | ENA

Pseudomonas jessenii strain:LMG 21605

Project description:Pseudomonas jessenii LMG 21605 genome sequencing

| PRJNA303778 | ENA

Pseudomonas jessenii strain:GO3

Project description:Pseudomonas jessenii strain:GO3 Genome sequencing and assembly

| PRJNA414171 | ENA

Pseudomonas jessenii strain:EC-S101

Project description:Pseudomonas jessenii strain:EC-S101 Genome sequencing and assembly

| PRJNA545876 | ENA

Pseudomonas jessenii strain:DSM 17150

Project description:Pseudomonas jessenii strain:DSM 17150 Genome sequencing and assembly

| PRJNA390484 | ENA

Proteomic analyses of Pseudomonas jessenii GO3 cells

Project description:Several soil organisms are known to be capable of growth on caprolactam as soil carbon and nitrogen source, but the enzymes of the catabolic pathway have not been described. We isolated a caprolactam-degrading strain of Pseudomonas jessenni, and identified genes putatively involved in the caprolactam metabolism using quantitative mass spectrometry-based proteomics. This led to the discovery of a caprolactamase and an aminotransferase that are involved in the initial steps of caprolactam conversion. Additionally, various proteins were identified likely to be involved in later steps of the pathway. The identified caprolactamase consisted of 2 subunits and demonstrated high sequence identity to the 5-oxoprolinases. E. coli expressing this caprolactamase did not convert 5-oxoproline but was able to hydrolyze caprolactam to form 6-aminohexanoic acid in an ATP dependent manner. Characterization of the aminotransferase revealed that the enzyme deaminated 6-aminohexanoic acid to produce 6-oxohexanoate with pyruvate as amino acceptor. The amino acid sequence of the aminotransferase demonstrated high similarity to subgroup II ω-aminotransferases of the PLP fold type I proteins. Finally, analyses of the genome sequence demonstrated the presence of a caprolactam catabolism gene cluster consisting of all genes involved in the conversion of caprolactam to adipate.

2018-10-22 | PXD008544 | Pride

Project description:Pseudomonas jessenii BS3660

| PRJEB16381 | ENA

Catalytic and structural properties of ATP-dependent caprolactamase from Pseudomonas jessenii.

Project description:Caprolactamase is the first enzyme in the caprolactam degradation pathway of Pseudomonas jessenii. It is composed of two subunits (CapA and CapB) and sequence-related to other ATP-dependent enzymes involved in lactam hydrolysis, like 5-oxoprolinases and hydantoinases. Low sequence similarity also exists with ATP-dependent acetone- and acetophenone carboxylases. The caprolactamase was produced in Escherichia coli, isolated by His-tag affinity chromatography, and subjected to functional and structural studies. Activity toward caprolactam required ATP and was dependent on the presence of bicarbonate in the assay buffer. The hydrolysis product was identified as 6-aminocaproic acid. Quantum mechanical modeling indicated that the hydrolysis of caprolactam was highly disfavored (ΔG0 '= 23 kJ/mol), which explained the ATP dependence. A crystal structure showed that the enzyme exists as an (αβ)2 tetramer and revealed an ATP-binding site in CapA and a Zn-coordinating site in CapB. Mutations in the ATP-binding site of CapA (D11A and D295A) significantly reduced product formation. Mutants with substitutions in the metal binding site of CapB (D41A, H99A, D101A, and H124A) were inactive and less thermostable than the wild-type enzyme. These residues proved to be essential for activity and on basis of the experimental findings we propose possible mechanisms for ATP-dependent lactam hydrolysis.

| S-EPMC8453981 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data