Universität zu Köln

Clermont, Lina, Macha, Arthur, Mueller, Laura M., Derya, Sami M., von Zaluskowski, Philipp, Eck, Alexander, Eikmanns, Bernhard J. and Seibold, Gerd M. (2015). The alpha-Glucan Phosphorylase MalP of Corynebacterium glutamicum Is Subject to Transcriptional Regulation and Competitive Inhibition by ADP-Glucose. J. Bacteriol., 197 (8). S. 1394 - 1408. WASHINGTON: AMER SOC MICROBIOLOGY. ISSN 1098-5530

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Abstract

alpha-Glucan phosphorylases contribute to degradation of glycogen and maltodextrins formed in the course of maltose metabolism in bacteria. Accordingly, bacterial alpha-glucan phosphorylases are classified as either glycogen or maltodextrin phosphorylase, GlgP or MalP, respectively. GlgP and MalP enzymes follow the same catalytic mechanism, and thus their substrate spectra overlap; however, they differ in their regulation: GlgP genes are constitutively expressed and the enzymes are controlled on the activity level, whereas expression of MalP genes are transcriptionally controlled in response to the carbon source used for cultivation. We characterize here the modes of control of the alpha-glucan phosphorylase MalP of the Gram-positive Corynebacterium glutamicum. In accordance to the proposed function of the malP gene product as MalP, we found transcription of malP to be regulated in response to the carbon source. Moreover, malP transcription is shown to depend on the growth phase and to occur independently of the cell glycogen content. Surprisingly, we also found MalP activity to be tightly regulated competitively by the presence of ADP-glucose, an intermediate of glycogen synthesis. Since the latter is considered a typical feature of GlgPs, we propose that C. glutamicum MalP acts as both maltodextrin and glycogen phosphorylase and, based on these findings, we question the current system for classification of bacterial alpha-glucan phosphorylases.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Clermont, Lina UNSPECIFIED UNSPECIFIED UNSPECIFIED Macha, Arthur UNSPECIFIED UNSPECIFIED UNSPECIFIED Mueller, Laura M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Derya, Sami M. UNSPECIFIED UNSPECIFIED UNSPECIFIED von Zaluskowski, Philipp UNSPECIFIED UNSPECIFIED UNSPECIFIED Eck, Alexander UNSPECIFIED UNSPECIFIED UNSPECIFIED Eikmanns, Bernhard J. UNSPECIFIED UNSPECIFIED UNSPECIFIED Seibold, Gerd M. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-408471
DOI:	10.1128/JB.02395-14
Journal or Publication Title:	J. Bacteriol.
Volume:	197
Number:	8
Page Range:	S. 1394 - 1408
Date:	2015
Publisher:	AMER SOC MICROBIOLOGY
Place of Publication:	WASHINGTON
ISSN:	1098-5530
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language CALLUNAE STARCH PHOSPHORYLASE; ESCHERICHIA-COLI; GLYCOGEN-PHOSPHORYLASE; CATALYTIC MECHANISM; ACETATE METABOLISM; BACTERIAL GLYCOGEN; MOLECULAR ANALYSIS; DIMER STRUCTURE; GLGX GENE; MALTOSE Multiple languages Microbiology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/40847