KEGG ENZYME: 2.4.1.359

ENZYME: 2.4.1.359

Entry

EC 2.4.1.359                Enzyme

Name

glucosylglycerol phosphorylase (configuration-retaining);
2-O-alpha-D-glucosylglycerol phosphorylase (retaining)

Class

Transferases;
Glycosyltransferases;
Hexosyltransferases

Sysname

2-O-alpha-D-glucopyranosyl-glycerol:phosphate alpha-D-glucosyltransferase (configuration-retaining)

Reaction(IUBMB)

2-O-alpha-D-glucopyranosyl-glycerol + phosphate = alpha-D-glucose 1-phosphate + glycerol [RN:R12243]

Reaction(KEGG)

R12243

Substrate

2-O-alpha-D-glucopyranosyl-glycerol [CPD:C11546];
phosphate [CPD:C00009]

Product

alpha-D-glucose 1-phosphate [CPD:C00103];
glycerol [CPD:C00116]

Comment

The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-alpha-D-glucopyranosyl-glycerol when the environmental salt concentration decreases. cf. EC 2.4.1.332, 1,2-alpha-glucosylglycerol phosphorylase.

History

EC 2.4.1.359 created 2018

Orthology

K23079

glucosylglycerol phosphorylase (configuration-retaining)

Genes

PCHE:

QYM18_01470(gtfA)

HPEG:

EAO82_11075(gtfA)

PNN:	KEM63_06870(gtfA)

MAD:	HP15_2853(gtfA)

MBS:	MRBBS_3760(gtfA)

MPQ:	ABA45_17615

MARI:

ACP86_04475

MSQ:	BKP64_07520

SNAN:

I6N98_14760(gtfA)

STAW:

NCG89_05015(gtfA)

FCE:	JN531_002590(gtfA)

» show all

Reference

1 [PMID:29470619]

Authors

Franceus J, Decuyper L, D'hooghe M, Desmet T

Title

Exploring the sequence diversity in glycoside hydrolase family 13_18 reveals a novel glucosylglycerol phosphorylase.

Journal

Appl Microbiol Biotechnol 102:3183-3191 (2018)
DOI:10.1007/s00253-018-8856-1

Sequence

[mad:HP15_2853]

Other DBs

ExplorEnz - The Enzyme Database:

2.4.1.359

IUBMB Enzyme Nomenclature:

2.4.1.359

ExPASy - ENZYME nomenclature database:

2.4.1.359

BRENDA, the Enzyme Database:

2.4.1.359

DBGET integrated database retrieval system