3.2.1.81: beta-agarase
This is an abbreviated version!
For detailed information about beta-agarase, go to the full flat file.
Word Map on EC 3.2.1.81
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3.2.1.81
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neoagarotetraose
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neoagarobiose
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agarolytic
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neoagarohexaose
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agar-degrading
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pseudoalteromonas
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agarivorans
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atlantica
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microbulbifer
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neoagaro-oligosaccharides
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galactanivorans
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gracilaria
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zobellia
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alteromonas
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catenovulum
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porphyran
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degradans
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saccharophagus
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flammeovirga
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carrageenase
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exo-type
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tat-dependent
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industry
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synthesis
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analysis
- 3.2.1.81
- neoagarotetraose
- neoagarobiose
- agarolytic
- neoagarohexaose
-
agar-degrading
- pseudoalteromonas
- agarivorans
- atlantica
- microbulbifer
- neoagaro-oligosaccharides
- galactanivorans
- gracilaria
- zobellia
- alteromonas
- catenovulum
- porphyran
- degradans
-
saccharophagus
- flammeovirga
-
carrageenase
-
exo-type
-
tat-dependent
- industry
- synthesis
- analysis
Reaction
Synonyms
AGA, Aga21, Aga50D, AgaA, AgaAc, AgaB, AgaB34, AgaC, AgaD, AgaP, agarase, Agarase 0107, agarase AG-a, AgaYT, beta-agarase, beta-agarase A, beta-agarase B, beta-agarase C, beta-agarase D, beta-agarase-a, DagA, endo-type beta-agarase, LSL-1, N3-1 protein, PjaA, RagaA11, YM01-1
ECTree
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Metals Ions
Metals Ions on EC 3.2.1.81 - beta-agarase
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Ba2+
Ca2+
CaCl2
K+
KCl
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no activity in the presence of 00.3 M salt. The enzyme shows a salt requirement for activity, being active from 0.3 M NaCl, with maximal activity at 3.5 M NaCl. KCl supports similar activities as NaCl up to 3.5 M, and LiCl up to 2.5 M. The monovalent salts can not be substituted by 3.5 M divalent cations, CaCl2 or MgCl2
LiCl
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no activity in the presence of 00.3 M salt. The enzyme shows a salt requirement for activity, being active from 0.3 M NaCl, with maximal activity at 3.5 M NaCl. KCl supports similar activities as NaCl up to 3.5 M, and LiCl up to 2.5 M. The monovalent salts can not be substituted by 3.5 M divalent cations, CaCl2 or MgCl2
Mg2+
Mn2+
Na+
NaCl
additional information
Ca2+
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the activity and stability of the wild type enzyme at 45°C with 1 mM CaCl2 are double those of the enzyme at 40°C without CaCl2. Activities of both the wild type and mutant E99K/T307I enzymes increase in 1 mM CaCl2. The E99K/T307I mutant enzyme is stable at 55°C with 1 mM CaCl2, reaching 260% of the activity the wild type enzyme held at 40°C without CaCl2. No further increases in activity are observed in 10 mMCaCl2
low concentration of Mn2+ have a slight positive effect on the AgaA activity (116% relative activity at 1 mM)
NaCl
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is required for activity, good production of agarase at NaCl concentration range from 1.5-3%. Maximum agarase production at 2.5% NaCl concentration
NaCl
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no activity in the presence of 0-0.3 M salt. The enzyme shows a salt requirement for activity, being active from 0.3 M NaCl, with maximal activity at 3.5 M NaCl. KCl supports similar activities as NaCl up to 3.5 M, and LiCl up to 2.5 M. The monovalent salts can not be substituted by 3.5 M divalent cations, CaCl2 or MgCl2
additional information
no activation of rAgaB34 by Na+, K+, Mg2+, Ca2+, and Ba2+
additional information
no significant activation or inhibition of AgaA is observed by Na+, K+, Ca2+, Fe3+, and urea
additional information
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not affected by 10 mM Mn2+, Na+, K+, Ca+, and Mg2+
additional information
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Ca2+, Mg2+, Ni2+, or Zn2+ do not affect on the activity at a concentration of 0.2 mM