Beta-glucosidase, chloroplastic precursor

Names and origin

Protein names

Recommended name:
    Beta-glucosidase, chloroplastic
    EC=3.2.1.21
Alternative name(s):
    Gentiobiase
    Cellobiase
    Beta-D-glucoside glucohydrolase

Gene names

Name:

GLU1

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

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Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Is implicated in many functions such as ABA metabolism, hydrolysis of conjugated gibberellins, conversion of storage forms of cytokinins to active forms. Also acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Enzyme regulation	Reversibly inhibited by micromolar concentrations of Hg(2+) or Ag(+), but irreversibly inhibited by alkylation in presence of urea. Competitive inhibition by p-nitrophenyl beta-D-thioglucoside (pNPTGlc), glucotetrazole, and para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin).
Subunit structure	Homodimer.
Subcellular location	Plastid › chloroplast.
Tissue specificity	Most abundant in the coleoptile.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.
Biophysicochemical properties	Kinetic parameters: K_M=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG) K_M=0.64 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) K_M=98 µM for DIMBOA-beta-D-glucoside pH dependence: Optimum pH is 5.8. Temperature dependence: Optimum temperature is 50 degrees Celsius. Loses activity when is heated at 55 degrees Celsius.

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Ontologies

Keywords
Biological process	Cytokinin signaling pathway
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Transit peptide

1 – 54

54

Chloroplast

Chain

55 – 566

512

Beta-glucosidase, chloroplastic

Regions

Region

325 – 361

37

Dimerization

Region

394 – 405

12

Dimerization

Region

450 – 453

4

Dimerization

Region

518 – 519

2

Substrate binding

Sites

Active site

245

1

Proton donor

Active site

460

1

Nucleophile

Binding site

92

1

Substrate

Binding site

387

1

Substrate

Binding site

511

1

Substrate

Amino acid modifications

Disulfide bond

264 ↔ 270

Experimental info

Mutagenesis

245

1

E → D or Q: Loss of activity

Mutagenesis

252

1

F → I, W or Y: Reduced substrate affinity

Mutagenesis

264

1

C → A, D, R or S: Loss of activity due to impaired dimerization

Mutagenesis

270

1

C → A, D, R or S: Loss of activity due to impaired dimerization

Mutagenesis

317

1

M → F, I or V: No effect

Mutagenesis

460

1

E → D: Loss of activity and impaired dimerization

Mutagenesis

460

1

E → Q: Loss of activity

Mutagenesis

463

1

I → D: Loss of activity due to impaired dimerization

Sequence conflict

477

1

A → D in CAA52293. Ref.2

Sequence conflict

551

1

E → Q in CAA52293. Ref.2

Sequence conflict

554

1

T → A in CAA52293. Ref.2

Secondary structure

1

.

566

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P49235-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4EA241258AE3641B
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FASTA

566

64,237

        10         20         30         40         50         60 
MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS FTTRSARVGS 

        70         80         90        100        110        120 
QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED GKGESNWDHF CHNHPERILD 

       130        140        150        160        170        180 
GSNSDIGANS YHMYKTDVRL LKEMGMDAYR FSISWPRILP KGTKEGGINP DGIKYYRNLI 

       190        200        210        220        230        240 
NLLLENGIEP YVTIFHWDVP QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW 

       250        260        270        280        290        300 
LTFNEPQTFT SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN 

       310        320        330        340        350        360 
KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG DYPFSMRSLA 

       370        380        390        400        410        420 
RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN YSPVLNTDDA YASQEVNGPD 

       430        440        450        460        470        480 
GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK YGNPPIYITE NGIGDVDTKE TPLPMEAALN 

       490        500        510        520        530        540 
DYKRLDYIQR HIATLKESID LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR 

       550        560 
YMKESAKWLK EFNTAKKPSK KILTPA

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References

[1]	Esen A., Shahid M. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Inbred line K55. Tissue: Shoot.
[2]	"Release of active cytokinin by a beta-glucosidase localized to the maize root meristem." Brzobohaty B., Moore I., Kristoffersen P., Bako L., Campos N., Schell J., Palme K. Science 262:1051-1054(1993) [PubMed: 8235622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. MUTIN. Tissue: Coleoptile.
[3]	"Purification and partial characterization of Maize (Zea Mays L.) beta-glucosidase." Esen A. Plant Physiol. 98:174-182(1992) [PubMed: 16668611] [Abstract] Cited for: PROTEIN SEQUENCE OF 55-74, CHARACTERIZATION. Strain: cv. Inbred line K55.
[4]	"The maize two dimensional gel protein database: towards an integrated genome analysis program." Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C., Zivy M., de Vienne D. Theor. Appl. Genet. 93:997-1005(1996) [Agricola: IND20551642] Cited for: PROTEIN SEQUENCE OF 55-69; 165-174; 207-213 AND 217-235. Tissue: Coleoptile.
[5]	"Expression, single-step purification, and matrix-assisted refolding of a maize cytokinin glucoside-specific beta-glucosidase." Zouhar J., Nanak E., Brzobohaty B. Protein Expr. Purif. 17:153-162(1999) [PubMed: 10497081] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside." Czjzek M., Cicek M., Zamboni V., Burmeister W.P., Bevan D.R., Henrissat B., Esen A. Biochem. J. 354:37-46(2001) [PubMed: 11171077] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 55-566 IN COMPLEX WITH THE INHIBITOR P-NITROPHENYL BETA-D-THIOGLUCOSIDE, ENZYME REGULATION, HOMODIMER, DISULFID BONDS.
[7]	"The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes." Czjzek M., Cicek M., Zamboni V., Bevan D.R., Henrissat B., Esen A. Proc. Natl. Acad. Sci. U.S.A. 97:13555-13560(2000) [PubMed: 11106394] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATES AND THE INHIBITOR PARA-HYDROXY-S-MANDELONITRILE BETA-GLUCOSIDE, MUTAGENESIS OF GLU-245, ENZYME REGULATION.
[8]	"Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1." Zouhar J., Vevodova J., Marek J., Damborsky J., Su X.-D., Brzobohaty B. Plant Physiol. 127:973-985(2001) [PubMed: 11706179] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 60-566, MUTAGENESIS OF GLU-245; PHE-252; MET-317; GLU-460 AND ILE-463, HOMODIMER, DISULFID BONDS.
[9]	"Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate." Verdoucq L., Moriniere J., Bevan D.R., Esen A., Vasella A., Henrissat B., Czjzek M. J. Biol. Chem. 279:31796-31803(2004) [PubMed: 15148317] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATES AND THE INHIBITOR GLUCOTETRAZOLE, MUTAGENESIS OF GLU-245, BIOPHYSICOCHEMICAL PROPERTIES, DISULFID BONDS.

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Cross-references

Sequence databases

U25157 mRNA. Translation: AAA65946.1.
X74217 mRNA. Translation: CAA52293.1.

PIR

A48860.

RefSeq

NP_001105454.1.

UniGene

Zm.94498

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E1E	X-ray	2.50	A/B	55-566	[»]
1E1F	X-ray	2.60	A/B	55-566	[»]
1E4L	X-ray	2.20	A/B	55-566	[»]
1E4N	X-ray	2.10	A/B	55-566	[»]
1E55	X-ray	2.00	A/B	55-566	[»]
1E56	X-ray	2.10	A/B	55-566	[»]
1H49	X-ray	1.90	A/B	55-566	[»]
1HXJ	X-ray	2.05	A/B	60-566	[

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases