产品名称
过氧化氢酶 来源于溶壁微球菌, solution, dark brown
SMILES string
O(CC)C(=O)c1ccc(cc1)O
InChI
1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3
InChI key
NUVBSKCKDOMJSU-UHFFFAOYSA-N
biological source
bacterial (Micrococcus lysodeikticus)
form
solution
specific activity
65,000-150,000 U/mL
mol wt
Mr ~230000
technique(s)
microbe id | metabolite detection: suitable
color
dark brown
solubility
0.05 M phosphate buffer pH 7.0: soluble, clear, brown (1:10)
Protein ID accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Application
裂解溶壁微球菌的过氧化氢酶已被用于通过体外生物催化级联消除糖类似物合成过程中过量的过氧化氢产生。它也被用作通过间接测量催化活性来评估氧化应激的标准。
Biochem/physiol Actions
过氧化氢酶能迅速将过氧化氢转化为氧气和水。它表现出抗氧化活性，并引发对活性氧（ROS）的防御机制。过氧化氢酶在自然界以及纺织、制药和乳制品等各种行业中起着中和有害过氧化氢的作用。微小球菌赖氨酸过氧化氢酶是一种含血红素的蛋白质。过氧化氢酶与参与过氧化氢（H2O2）处理的多种关键细胞系统一起，在调节细胞氧化还原平衡和辅助细胞和细胞间信号传递方面起着关键作用。
General description
研究领域：细胞信号传导
过氧化氢酶（CAT）是一种抗氧化酶，由CAT基因家族编码。该酶在大多数好氧生物中普遍存在。
过氧化氢酶（CAT）是一种抗氧化酶，由CAT基因家族编码。该酶在大多数好氧生物中普遍存在。
Other Notes
1U对应于在pH7.0和25℃下，每分钟分解1 μmol H2O2 所需的酶量
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
法规信息
常规特殊物品
常规特殊物品
此项目有
J Bravo et al.
Structure (London, England : 1993), 3(5), 491-502 (1995-05-15)
Catalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. It serves, in part, to protect the cell from the toxic effects of small peroxides. Escherichia coli produces two catalases, HPI and HPII, that
Catalase (CAT) Gene Family in Rapeseed (Brassica napus L.): Genome-Wide Analysis, Identification, and Expression Pattern in Response to Multiple Hormones and Abiotic Stress Conditions
Raza A, et al.
International Journal of Molecular Sciences, 22(8) (2021)
Catalase: A critical node in the regulation of cell fate
Baker A, et al.
Free Radical Biology & Medicine, 56-66 (2023)
Hessam Sepasi Tehrani et al.
Progress in biophysics and molecular biology, 140, 5-12 (2018-03-14)
Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing
Ivan Gomez-Mestre et al.
PloS one, 8(12), e84266-e84266 (2013-12-21)
Many amphibian species exploit temporary or even ephemeral aquatic habitats for reproduction by maximising larval growth under benign conditions but accelerating development to rapidly undergo metamorphosis when at risk of desiccation from pond drying. Here we determine mechanisms enabling developmental
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