Literature summary for 3.7.1.24 extracted from

Zhang, Z.; Jiang, Y.L.; Wu, Y.; He, Y.X.
Crystallization and preliminary X-ray diffraction analysis of a putative carbon-carbon bond hydrolase from Mycobacterium abscessus 103 (2015), Acta Crystallogr. Sect. F, 71, 239-242.

Search for more literature for 3.7.1.24

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression	Mycobacteroides abscessus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, using a precipitant consisting of 100 mM citric acid, pH 5.0, 1.0 M lithium chloride, 8% w/v PEG 6000, X-ray diffraction structure determination and analysis at 1.87 A resolution	Mycobacteroides abscessus

Organism

Organism	UniProt	Comment	Textmining
Mycobacteroides abscessus	-	-	-
Mycobacteroides abscessus 103	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Mycobacteroides abscessus

Synonyms

Synonyms	Comment	Organism
mPhlG	-	Mycobacteroides abscessus

General Information

General Information	Comment	Organism
evolution	the PhlG protein from Mycobacterium abscessus 103 (mPhlG), which shares 30% sequence identity with phloretin hydrolase from Eubacterium ramulus and 38% sequence identity with 2,4-diacetylphloroglucinol hydrolase from Pseudomonas fluorescens Pf-5, is a putative carbon-carbon bond hydrolase	Mycobacteroides abscessus

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Release 2023.1 (January 2023)