Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Homo sapiens

ABSTRACT: Exome Sequencing for Metastatic Colorectal Cancer

PROVIDER: PRJNA726023 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR14463500_1.fastq.gz	Fastqsanger.gz
	SRR14463500_2.fastq.gz	Fastqsanger.gz
	SRR14463501_1.fastq.gz	Fastqsanger.gz
	SRR14463501_2.fastq.gz	Fastqsanger.gz
	SRR14463502_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 154

Similar Datasets

Homo sapiens

Project description:Genomic landscape of metastatic colorectal cancer

| PRJNA156909 | ENA

Homo sapiens

Project description:Whole Exome Sequencing of Colorectal Cancer

| PRJNA1077689 | ENA

Homo sapiens

Project description:Exome sequencing of metastatic ovarian cancer samples

| PRJNA281537 | ENA

Homo sapiens

Project description:CIDR: Whole Exome Sequencing for Colorectal Cancer

| PRJNA75823 | ENA

Homo sapiens

Project description:microRNA data in human metastatic versus non-metastatic colorectal cancer tissues

| PRJNA360836 | ENA

Homo sapiens

Project description:Comparative Sequencing Analysis Between Primary and Metastatic Colorectal Cancer Lesions

| PRJNA258567 | ENA

Homo sapiens

Project description:Comparative Sequencing Analysis Between Primary and Metastatic Colorectal Cancer Lesions

| PRJNA258568 | ENA

Homo sapiens

Project description:Whole Exome Sequencing of Colorectal Cancer Epidemiologic Cohorts

| PRJNA239537 | ENA

Homo sapiens

Project description:Whole exome sequencing of Colorectal Cancer Liver Metastases

| PRJNA505117 | ENA

Crystal structure of Homo sapiens kynureninase.

Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

| S-EPMC2531291 | 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