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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: amylopullulanase

Gene: apu Accession Number: G-12577 (MetaCyc)

Synonyms: PF1935*

Species: Pyrococcus furiosus DSM 3638

Summary:
The subunit structure of this protein has not been reported.

The asterisk in PF1935* reflects the correction of a genome sequence error. The correction combines PF1935 with PF1934 into a single, continuous gene designated PF1935* [Lee06a].

This is a highly thermostable enzyme from a hyperthermophilic archaeon. It belongs to the glycosyl hydrolase family 57. Such enzymes are of interest in industrial starch conversion. Thermostable amylopullulanases have been characterized from several anaerobic, thermophilic bacteria and hyperthermophilic archaea. These enzymes are able to hydrolyze both α-1,4 and α-1,6 linkages (in [Dong97]).

The enzyme activity data shown here are for truncated, recombinant forms of the enzyme that contain the catalytic domain [Kang05a, Dong97]. Site-directed mutagenesis studies have identified catalytically important residues [Kang05a].

Molecular Weight of Polypeptide: 127.21 kD (from nucleotide sequence)

Unification Links: Entrez-Nucleotide:DQ192527 , Pride:Q3HUR3 , String:Q3HUR3 , UniProt:Q3HUR3

Relationship Links: CAZy:IN-FAMILY:GH57 , InterPro:IN-FAMILY:IPR004300 , InterPro:IN-FAMILY:IPR010502 , InterPro:IN-FAMILY:IPR011330 , InterPro:IN-FAMILY:IPR019248 , InterPro:IN-FAMILY:IPR027291 , InterPro:IN-FAMILY:IPR027552 , Pfam:IN-FAMILY:PF03065 , Pfam:IN-FAMILY:PF09985

Gene-Reaction Schematic: ?

Credits:
Created 01-Mar-2011 by Fulcher CA , SRI International


Enzymatic reaction of: pullulanase

a large-branched glucan + n H2O <=> n a long-linear glucan

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for a large-branched glucan: amylopectin [Dong97 ]

Summary:
In addition to α-amylase activity, the enzyme also had pullulanase activity which produced maltotriose and maltose as 87% and 10% of the total products [Kang05a, Dong97].

Activators (Unknown Mechanism): Ca2+ [Dong97] , Sr2+ [Dong97]

Inhibitors (Unknown Mechanism): a cyclodextrin [Dong97] , EDTA [Dong97] , Ni2+ [Dong97] , Cu2+ [Dong97] , Zn2+ [Dong97]

T(opt): 105 °C [Dong97]

pH(opt): 6.0 [Dong97]


Enzymatic reaction of: α-amylase (amylopullulanase)

EC Number: 3.2.1.-

starch[extracellular space] + H2O[extracellular space] <=> a maltodextrin(n)[extracellular space] + maltose[extracellular space] + D-glucopyranose[extracellular space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for starch: α-amylose [Dong97 ]

In Pathways: starch degradation V

Summary:
In vitro the α-amylase activity of the enzyme hydrolyzed soluble starch to a mixture of mainly maltohexaose, maltopentaose, maltotetraose, maltotriose, maltose and D-glucose). The enzyme also hydrolyzed oligosaccharide substrates, but more slowly than longer chain molecules [Dong97].


References

Dong97: Dong G, Vieille C, Zeikus JG (1997). "Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme." Appl Environ Microbiol 63(9);3577-84. PMID: 9293009

Kang05a: Kang S, Vieille C, Zeikus JG (2005). "Identification of Pyrococcus furiosus amylopullulanase catalytic residues." Appl Microbiol Biotechnol 66(4);408-13. PMID: 15599521

Lee06a: Lee HS, Shockley KR, Schut GJ, Conners SB, Montero CI, Johnson MR, Chou CJ, Bridger SL, Wigner N, Brehm SD, Jenney FE, Comfort DA, Kelly RM, Adams MW (2006). "Transcriptional and biochemical analysis of starch metabolism in the hyperthermophilic archaeon Pyrococcus furiosus." J Bacteriol 188(6);2115-25. PMID: 16513741


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc14.