Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.92 - kanosamine-6-phosphate phosphatase and Organism(s) Bacillus subtilis and UniProt Accession O07565

for references in articles please use BRENDA:EC3.1.3.92
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.92 kanosamine-6-phosphate phosphatase
IUBMB Comments
The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: O07565
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
kanosamine-6-phosphate phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ntdB
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
kanosamine-6-phosphate phosphohydrolase
The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucosamine 6-phosphate + H2O
D-glucosamine + phosphate
show the reaction diagram
about 1% of the activity with kanosamine 6-phosphate
-
-
?
kanosamine 6-phosphate + H2O
kanosamine + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.101
kanosamine 6-phosphate
pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
32
kanosamine 6-phosphate
pH not specified in the publication, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the ntd operon is essential for biosynthesis of the unusual disaccharide 3,3'-neotrehalosadiamine. The enzymes catalyze the biosynthesis of kanosamine from glucose 6-phosphate. NtdC is a glucose-6-phosphate 3-dehydrogenase, NtdA is a pyridoxal phosphate-dependent 3-oxo-glucose-6-phosphate:glutamate aminotransferase, and NtdB is a kanosamine-6-phosphate phosphatase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in 'Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vetter, N.D.; Langill, D.M.; Anjum, S.; Boisvert-Martel, J.; Jagdhane, R.C.; Omene, E.; Zheng, H.; van Straaten, K.E.; Asiamah, I.; Krol, E.S.; Sanders, D.A.; Palmer, D.R.
A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis
J. Am. Chem. Soc.
135
5970-5973
2013
Bacillus subtilis (O07565), Bacillus subtilis
Manually annotated by BRENDA team